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Stephen K Farrand - One of the best experts on this subject based on the ideXlab platform.
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Co-evolution of the agrocinOpine Opines and the agrocinOpine-mediated control of TraR, the quorum- sensing activator of the Ti plasmid conjugation system
Molecular Microbiology, 2008Co-Authors: Philippe Oger, Stephen K FarrandAbstract:Summary Conjugal transfer of Agrobacterium tumefaciens Ti plasmids is controlled by a hierarchical system in which Opines, substrates produced by crown gall tumours, induce a quorum-sensing system. The cascade results from the control of expression of traR, the quorum-sensing activator, by a regulator responsive to the Opine. In the two cases studied to date, the gene arrangements responsible for the cascade differ remarkably, suggesting that considerable diversity exists among the many Ti-like plasmids in the agrobacteria. In this study, we demonstrated that the novel Ti plasmid pTiChry5 is induced to transfer at high frequency by extracts from tumours initiated by strain Chry5. The purified inducer had the chemical and biological properties of agrocinOpines C and D, a set of sugar phosphodiester Opines known to induce transfer of another Ti plasmid, pTiBo542. The T-region of pTiChry5 contained a gene whose product, called AcsChry5, is virtually identical to the agrocinOpine C1D synthase from the T-region of pTiBo542. The two genes are less closely related to acs of pTiC58, which is responsible for the production of agrocinOpines A1B, a similar but not identical set of phosphodiester Opines by tumours induced by strain C58. AgrocinOpines A1B induce transfer of pTiC58 but did not induce transfer of pTiChry5. A single copy of traR was identified at the 11 o’clock region of pTiChry5, where it is part of a two-gene operon called arcChry5. Although altered by deletions, arcChry5 is related to the five-gene arc operon that controls the expression of traR on pTiC58. Expression of traRChry5 was induced by agrocinOpines C1D and the Opines isolated from Chry5 tumours but not by agrocinOpines A1B. A mutation in traRChry5 abolished transfer, and transfer was restored by complementation in trans. We conclude that the agrocinOpine Opines and the corresponding Opine-meditated conjugal regulatory regions of pTiChry5 and pTiC58 share a common origin, but that the Opine signals for the two Ti plasmids have evolved divergently through changes in the Opine synthase enzymes. The alterations in the Opines, in turn, necessitated a coevolutionary change in the Opine recognition systems responsible for controlling expression of the traR genes on these two types of Ti plasmids.
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Opine based agrobacterium competitiveness dual expression control of the agrocinOpine catabolism acc operon by agrocinOpines and phosphate levels
Journal of Bacteriology, 2008Co-Authors: Hyojeong Yi, Jaehee Myung, Kevin R Piper, Stephen K FarrandAbstract:Agrobacterium tumefaciens strain C58 can transform plant cells to produce and secrete the sugar-phosphate conjugate Opines agrocinOpines A and B. The bacterium then moves in response to the Opines and utilizes them as exclusive sources of carbon, energy, and phosphate via the functions encoded by the acc operon. These privileged Opine-involved activities contribute to the formation of agrobacterial niches in the environment. We found that the expression of the acc operon is induced by agrocinOpines and also by limitation of phosphate. The main promoter is present in front of the first gene, accR, which codes for a repressor. This operon structure enables efficient repression when Opine levels are low. The promoter contains two putative operators, one overlapping the −10 sequence and the other in the further upstream from it; two partly overlapped putative pho boxes between the two operators; and two consecutive transcription start sites. DNA fragments containing either of the operators bound purified repressor AccR in the absence of agrocinOpines but not in the presence of the Opines, demonstrating the on-off switch of the promoter. Induction of the acc operon can occur under low-phosphate conditions in the absence of agrocinOpines and further increases when the Opines also are present. Such Opine-phosphate dual regulatory system of the operon may ensure maximum utilization of agrocinOpines when available and thereby increase the chances of agrobacterial survival in the highly competitive environment with limited general food sources.
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Two Opines Control Conjugal Transfer of an Agrobacterium Plasmid by Regulating Expression of Separate Copies of the Quorum-Sensing Activator Gene traR
Journal of Bacteriology, 2002Co-Authors: Philippe Oger, Stephen K FarrandAbstract:Conjugal transfer of Ti plasmids from Agrobacterium spp. is controlled by a hierarchical regulatory system designed to sense two environmental cues. One signal, a subset of the Opines produced by crown gall tumors initiated on plants by the pathogen, serves to induce production of the second, an acyl-homoserine lactone quorum-sensing signal, the quormone, produced by the bacterium itself. This second signal activates TraR, and this transcriptional activator induces expression of the tra regulon. Opines control transfer because the traR gene is a member of an operon the expression of which is regulated by the conjugal Opine. Among the Ti plasmid systems studied to date, only one of the two or more Opine families produced by the associated tumor induces transfer. However, two chemically dissimilar Opines, nopaline and agrocinOpines A and B, induce transfer of the Opine catabolic plasmid pAtK84b found in the nonpathogenic Agrobacterium radiobacter isolate K84. In this study we showed that this plasmid contains two copies of traR, and each is associated with a different Opine-regulated operon. One copy, traRnoc, is the last gene of the nox operon and was induced by nopaline but not by agrocinOpines A and B. Mutating traRnoc abolished induction of transfer by nopaline but not by the agrocinOpines. A mutation in ocd, an upstream gene of the nox operon, abolished utilization of nopaline and also induction of transfer by this Opine. The second copy, traRacc, is located in an operon of four genes and was induced by agrocinOpines A and B but not by nopaline. Genetic analysis indicated that this gene is required for induction of transfer by agrocinOpines A and B but not by nopaline. pAtK84b with mutations in both traR genes was not induced for transfer by either Opine. However, expression of a traR gene in trans to this plasmid resulted in Opine-independent transfer. The association of traRnoc with nox is unique, but the operon containing traRacc is related to the arc operons of pTiC58 and pTiChry5, two Ti plasmids inducible for transfer by agrocinOpines A-B and C-D, respectively. We conclude that pAtK84b codes for two independently functioning copies of traR, each regulated by a different Opine, thus accounting for the activation of the transfer system of this plasmid by the two Opine types.
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intracellular accumulation of mannOpine an Opine produced by crown gall tumors transiently inhibits growth of agrobacterium tumefaciens
Molecular Plant-microbe Interactions, 2001Co-Authors: Changho Baek, Jai Myung Yang, Stephen K FarrandAbstract:pYDH208, a cosmid clone from the octOpine-mannityl Opine-type tumor-inducing (Ti) plasmid pTi15955 confers utilization of mannOpine (MOP) and agrOpine (AGR) on Agrobacterium tumefaciens strain NT1. NT1 harboring pYDH208 with an insertion mutation in mocC, which codes for MOP oxidoreductase, not only fails to utilize MOP as a sole carbon source, but also was inhibited in its growth by MOP and AGR. In contrast, the growth of mutants with insertions in other tested moc genes was not inhibited by either Opine. Growth of strains NT1 or UIA5, a derivative of C58 that lacks pAtC58, was not inhibited by MOP, but growth of NT1 or UIA5 harboring pRE10, which codes for the MOP transport system, was inhibited by the Opine. When a clone expressing mocC was introduced, the growth of strain NT1(pRE10) was not inhibited by MOP, although UIA5(pRE10) was still weakly inhibited. In strain NT1(pRE10, mocC), santhOpine (SOP), produced by the oxidation of MOP by MocC, was further degraded by functions encoded by pAtC58. These ...
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hierarchical gene regulatory systems arising from fortuitous gene associations controlling quorum sensing by the Opine regulon in agrobacterium
Molecular Microbiology, 1999Co-Authors: Kevin R Piper, Susanne B Von Bodman, Ingyu Hwang, Stephen K FarrandAbstract:Conjugation of the Agrobacterium Ti plasmid pTiC58 is regulated by a hierarchy involving induction by the Opines agrocinOpines A and B and a quorum-sensing system. Regulation by the Opines is mediated by the repressor AccR, while quorum sensing is effected by the transcriptional activator TraR and its ligand, the acyl-homoserine lactone signal molecule Agrobacterium autoinducer (AAI). These last two elements combine to activate expression of the tra system at high population densities. Sequence analysis indicated that traR is the fourth gene of an operon, which we named arc, that is transcribed divergently from accR. Complementation analysis of mutations in the genes 5′ to traR showed that the other members of the arc operon are not required for conjugation. Analysis of lacZ reporter fusions demonstrated that traR expression is regulated directly by AccR. Deletion analysis showed that AccR-regulated expression of traR initiates from a promoter located in the intergenic region between accR and orfA, the first gene of the arc operon. Reverse transcriptase–polymerase chain reaction (RT–PCR) and primer extension analyses indicated that the arc transcript initiates upstream of orfA and proceeds uninterrupted through traR. These results are consistent with a model in which quorum sensing is subordinate to the Opine regulon because traR has become associated with an operon controlled by the Opine-responsive transcriptional regulator.
Yasuhisa Asano - One of the best experts on this subject based on the ideXlab platform.
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Opine dehydrogenase secondary amine dicarboxylic acids
Encyclopedia of Industrial Biotechnology, 2010Co-Authors: Yasuo Kato, Yasuhisa AsanoAbstract:Naturally Occurring Opines Secondary Amine Dicarboxylic Acids Enzymes Acting on Secondary Amine Dicarboxylic Acids Opine Dehydrogenase from Arthrobacter sp. Strain 1C Isolation of (1-d-Carboxyethyl)-l-Phenylalanine-Assimilating Bacteria Purification of Opine Dehydrogenase from Arthrobacter sp. Strain 1C Cloning, Nucleotide Sequencing, and Expression of Opine Dehydrogenase Stereoselective Synthesis of Opine-Type Secondary Amine Carboxylic Acids by Opine Dehydrogenase Conclusion Bibliography Keywords: amino acid dehydrogenase; enzymatic synthesis; enzyme purification and properties; Opine compound; Opine dehydrogenase; secondary amine dicarboxylic acid
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Encyclopedia of Industrial Biotechnology - Opine Dehydrogenase, Secondary Amine Dicarboxylic Acids
Encyclopedia of Industrial Biotechnology, 2010Co-Authors: Yasuo Kato, Yasuhisa AsanoAbstract:Naturally Occurring Opines Secondary Amine Dicarboxylic Acids Enzymes Acting on Secondary Amine Dicarboxylic Acids Opine Dehydrogenase from Arthrobacter sp. Strain 1C Isolation of (1-d-Carboxyethyl)-l-Phenylalanine-Assimilating Bacteria Purification of Opine Dehydrogenase from Arthrobacter sp. Strain 1C Cloning, Nucleotide Sequencing, and Expression of Opine Dehydrogenase Stereoselective Synthesis of Opine-Type Secondary Amine Carboxylic Acids by Opine Dehydrogenase Conclusion References Keywords: amino acid dehydrogenase; enzymatic synthesis; enzyme purification and properties; Opine compound; Opine dehydrogenase; secondary amine dicarboxylic acid
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a japanese screening approach selection of an Opine dehydrogenase and alkaline d peptidase
Studies in organic chemistry, 1998Co-Authors: Yasuhisa AsanoAbstract:Publisher Summary This chapter examines a Japanese screening approach, which includes selection of Opine dehydrogenase and alkaline D-peptidase. It introduces enrichment and acclimation techniques with the isolation of nitrile degraders as typical examples. Enrichment culture technique is a method to isolate microorganisms having a specific ability to grow on a medium which has a specified feature in its composition and conditions, such as carbon and nitrogen sources, pH, temperature, and aeration. Microorganisms growing faster than the other species become dominant in the culture. Acclimation technique is run with a toxic or unnatural compound as a substrate and usually with a longer term to isolate microorganisms which are not easily isolated by the enrichment culture technique. Opine-type secondary amine dicarboxylic acids are useful chiral intermediates of angiotensin-converting enzyme (ACE)-inhibitors, such as enalapril and lysinopril. A novel NAD + -dependent Opine dehydrogenase is purified to homogeneity from Arthrobacter sp. strain 1C isolated from soil by an enrichment culture technique with a synthetic substrate N-[1-DL-(carboxyl)ethyl]-L-phenylalanine.
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stereoselective synthesis of Opine type secondary amine car ylic acids by a new enzyme Opine dehydrogenase use of recombinant enzymes
Journal of Molecular Catalysis B-enzymatic, 1996Co-Authors: Yasuo Kato, Hideaki Yamada, Yasuhisa AsanoAbstract:Abstract The substrate specificity of the recently discovered enzyme, Opine dehydrogenase (ODH) fromArthrobacter sp. strain 1C for amino donors in the reaction that forms secondary amines using pyruvate as a fixed amino acceptor is examined. The enzyme was active toward short-chain aliphatic (S)-amino acids and those substituted with acyloxy, phosphonooxy, and halogen groups. The enzyme was named N-[1-(R)-(car☐yl)ethyl]-(S)-norvaline: NAD+ oxidoreductase (L-norvaline forming). Other substrates for the enzyme were 3-aminobutyric acid and (S)-phenylalaninol. Optically pure Opine-type secondary amine car☐ylic acids were synthesized from amino acids and their analogs such as (S)-methionine, (S)-isoleucine, (S)-leucine, (S)-valine, (S)-phenylalanine, (S)-alanine, (S)-threonine, (S)-serine, and (S)-phenylalaninol, and α-keto acids such as glyoxylate, pyruvate, and 2-oxobutyrate using the enzyme, with regeneration of NADH by formate dehydrogenase (FDH) fromMoraxella sp. C-1. The absolute configuration of the nascent asymmetric center of the Opines was of the (R) stereochemistry with > 99.9% e.e. One-pot synthesis of N-[1-(R)-(car☐yl)ethyl]-(S)-phenylalanine from phenylpyruvate and pyruvate by using ODH, FDH, and phenylalanine dehydrogenase (PheDH) fromBacillus sphaericus, is also described.
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Stereoselective synthesis of Opine-type secondary amine car☐ylic acids by a new enzyme Opine dehydrogenase use of recombinant enzymes
Journal of Molecular Catalysis B-enzymatic, 1996Co-Authors: Yasuo Kato, Hideaki Yamada, Yasuhisa AsanoAbstract:Abstract The substrate specificity of the recently discovered enzyme, Opine dehydrogenase (ODH) fromArthrobacter sp. strain 1C for amino donors in the reaction that forms secondary amines using pyruvate as a fixed amino acceptor is examined. The enzyme was active toward short-chain aliphatic (S)-amino acids and those substituted with acyloxy, phosphonooxy, and halogen groups. The enzyme was named N-[1-(R)-(car☐yl)ethyl]-(S)-norvaline: NAD+ oxidoreductase (L-norvaline forming). Other substrates for the enzyme were 3-aminobutyric acid and (S)-phenylalaninol. Optically pure Opine-type secondary amine car☐ylic acids were synthesized from amino acids and their analogs such as (S)-methionine, (S)-isoleucine, (S)-leucine, (S)-valine, (S)-phenylalanine, (S)-alanine, (S)-threonine, (S)-serine, and (S)-phenylalaninol, and α-keto acids such as glyoxylate, pyruvate, and 2-oxobutyrate using the enzyme, with regeneration of NADH by formate dehydrogenase (FDH) fromMoraxella sp. C-1. The absolute configuration of the nascent asymmetric center of the Opines was of the (R) stereochemistry with > 99.9% e.e. One-pot synthesis of N-[1-(R)-(car☐yl)ethyl]-(S)-phenylalanine from phenylpyruvate and pyruvate by using ODH, FDH, and phenylalanine dehydrogenase (PheDH) fromBacillus sphaericus, is also described.
Yves Dessaux - One of the best experts on this subject based on the ideXlab platform.
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Import pathways of the mannityl-Opines into the bacterial pathogen Agrobacterium tumefaciens: structural, affinity and in vivo approaches.
Biochemical Journal, 2020Co-Authors: Armelle Vigouroux, Yves Dessaux, Loic Marty, Magali Aumont-nicaise, Jeanne Doré, Pierre Legrand, Ludovic Vial, Solange MoréraAbstract:Agrobacterium tumefaciens pathogens use specific compounds denoted Opines as nutrients in their plant tumor niche. These Opines are produced by the host plant cells genetically modified by agrobacteria. They are imported into bacteria via solute-binding proteins (SBPs) in association with ABC transporters. The mannityl-Opine family encompasses mannOpine, mannopinic acid, agrOpine and agropinic acid. Structural and affinity data on mannopinic acid bound to SBPs are currently lacking while those of the three others mannityl Opines are available. We investigated the molecular basis of two pathways for mannopinic acid uptake. MoaA was proposed as the specific SBP for mannopinic acid import in mannityl Opines-assimilating agrobacteria, which was validated here using genetic studies and affinity measurements. We structurally characterized the mannopinic acid binding mode of MoaA in two crystal forms at 2.05 and 1.57 A resolution. We demonstrated that the non-specific SBP MotA, so far characterized as mannOpine and Amadori compound importer, was also able to transport mannopinic acid. The structure of MotA bound to mannopinic acid at 2.2 A resolution defines a different mannopinic acid binding signature, similar to that of mannOpine. Combining in vitro and in vivo approaches, this work allowed us to complete the characterization of the mannityl-Opines assimilation pathways, highlighting the important role of two dual imports of agropinic and mannopinic acids. Our data shed new light on how the mannityl-Opines contribute to the establishment of the ecological niche of agrobacteria from the early to the late stages of tumor development.
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structural basis for two efficient modes of agropinic acid Opine import into the bacterial pathogen agrobacterium tumefaciens
Biochemical Journal, 2018Co-Authors: Loic Marty, Yves Dessaux, Armelle Vigouroux, Magali Aumontnicaise, Franck Pelissier, Thibault Meyer, Celine Lavire, S MoreraAbstract:Agrobacterium tumefaciens pathogens genetically modify their host plants to drive the synthesis of Opines in plant tumors. The mannityl-Opine family encompasses mannOpine, mannopinic acid, agrOpine and agropinic acid. These Opines serve as nutrients and are imported into bacteria via periplasmic-binding proteins (PBPs) in association with ABC transporters. Structural and affinity data on agrOpine and agropinic acid Opines bound to PBPs are currently lacking. Here, we investigated the molecular basis of AgtB and AgaA, proposed as the specific PBP for agrOpine and agropinic acid import, respectively. Using genetic approaches and affinity measurements, we identified AgtB and its transporter as responsible for agrOpine uptake in agrOpine-assimilating agrobacteria. Nonetheless, we showed that AgtB binds agropinic acid with a higher affinity than agrOpine, and we structurally characterized the agropinic acid-binding mode through three crystal structures at 1.4, 1.74 and 1.9 A resolution. In the crystallization time course, obtaining a crystal structure of AgtB with agrOpine was unsuccessful due to the spontaneous lactamization of agrOpine into agropinic acid. AgaA binds agropinic acid only with a similar affinity in nanomolar range as AgtB. The structure of AgaA bound to agropinic acid at 1.65 A resolution defines a different agropinic acid-binding signature. Our work highlights the structural and functional characteristics of two efficient agropinic acid assimilation pathways, of which one is also involved in agrOpine assimilation.
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structural basis for high specificity of amadori compound and mannOpine Opine binding in bacterial pathogens
Journal of Biological Chemistry, 2016Co-Authors: Loic Marty, Yves Dessaux, Armelle Vigouroux, Magali Aumontnicaise, Denis Faure, S MoreraAbstract:Agrobacterium tumefaciens pathogens genetically modify their host plants to drive the synthesis of Opines in plant tumors. Opines are either sugar phosphodiesters or the products of condensed amino acids with ketoacids or sugars. They are Agrobacterium nutrients and imported into the bacterial cell via periplasmic-binding proteins (PBPs) and ABC-transporters. MannOpine, an Opine from the mannityl-Opine family, is synthesized from an intermediate named deoxy-fructosyl-glutamine (DFG), which is also an Opine and abundant Amadori compound (a name used for any derivative of aminodeoxysugars) present in decaying plant materials. The PBP MotA is responsible for mannOpine import in mannOpine-assimilating agrobacteria. In the nopaline-Opine type agrobacteria strain, SocA protein was proposed as a putative mannOpine binding PBP, and AttC protein was annotated as a mannOpine binding-like PBP. Structural data on mannityl-Opine-PBP complexes is currently lacking. By combining affinity data with analysis of seven x-ray structures at high resolution, we investigated the molecular basis of MotA, SocA, and AttC interactions with mannOpine and its DFG precursor. Our work demonstrates that AttC is not a mannOpine-binding protein and reveals a specific binding pocket for DFG in SocA with an affinity in nanomolar range. Hence, mannOpine would not be imported into nopaline-type agrobacteria strains. In contrast, MotA binds both mannOpine and DFG. We thus defined one mannOpine and two DFG binding signatures. Unlike mannOpine-PBPs, selective DFG-PBPs are present in a wide diversity of bacteria, including Actinobacteria, α-,β-, and γ-proteobacteria, revealing a common role of this Amadori compound in pathogenic, symbiotic, and opportunistic bacteria.
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Agrobacterium uses a unique ligand-binding mode for trapping Opines and acquiring a competitive advantage in the niche construction on plant host.
PLOS Pathogens, 2014Co-Authors: Julien Lang, Yves Dessaux, Armelle Vigouroux, Sara Planamente, Abbas El Sahili, Pauline Blin, Magali Aumont-nicaise, Solange Moréra, Denis FaureAbstract:By modifying the nuclear genome of its host, the plant pathogen Agrobacterium tumefaciens induces the development of plant tumours in which it proliferates. The transformed plant tissues accumulate uncommon low molecular weight compounds called Opines that are growth substrates for A. tumefaciens. In the pathogen-induced niche (the plant tumour), a selective advantage conferred by Opine assimilation has been hypothesized, but not experimentally demonstrated. Here, using genetics and structural biology, we deciphered how the pathogen is able to bind Opines and use them to efficiently compete in the plant tumour. We report high resolution X-ray structures of the periplasmic binding protein (PBP) NocT unliganded and liganded with the Opine nopaline (a condensation product of arginine and α-ketoglurate) and its lactam derivative pyronopaline. NocT exhibited an affinity for pyronopaline (KD of 0.6 µM) greater than that for nopaline (KD of 3.7 µM). Although the binding-mode of the arginine part of nopaline/pyronopaline in NocT resembled that of arginine in other PBPs, affinity measurement by two different techniques showed that NocT did not bind arginine. In contrast, NocT presented specific residues such as M117 to stabilize the bound Opines. NocT relatives that exhibit the nopaline/pyronopaline-binding mode were only found in genomes of the genus Agrobacterium. Transcriptomics and reverse genetics revealed that A. tumefaciens uses the same pathway for assimilating nopaline and pyronopaline. Fitness measurements showed that NocT is required for a competitive colonization of the plant tumour by A. tumefaciens. Moreover, even though the Ti-plasmid conjugal transfer was not regulated by nopaline, the competitive advantage gained by the nopaline-assimilating Ti-plasmid donors led to a preferential horizontal propagation of this Ti-plasmid amongst the agrobacteria colonizing the plant-tumour niche. This work provided structural and genetic evidences to support the niche construction paradigm in bacterial pathogens.
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engineered rhizosphere the trophic bias generated by Opine producing plants is independent of the Opine type the soil origin and the plant species
Applied and Environmental Microbiology, 2002Co-Authors: Hounayda Mansouri, Annik Petit, Phil M Oger, Yves DessauxAbstract:In a previous study, we demonstrated that transgenic Lotus plants producing Opines (which are small amino acid and sugar conjugates) specifically favor growth of Opine-degrading rhizobacteria. The Opine-induced bias was repeated and demonstrated with another soil type and another plant species (Solanum nigrum). This phenomenon is therefore independent of both soil type and plant species.
Yasuo Kato - One of the best experts on this subject based on the ideXlab platform.
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Opine dehydrogenase secondary amine dicarboxylic acids
Encyclopedia of Industrial Biotechnology, 2010Co-Authors: Yasuo Kato, Yasuhisa AsanoAbstract:Naturally Occurring Opines Secondary Amine Dicarboxylic Acids Enzymes Acting on Secondary Amine Dicarboxylic Acids Opine Dehydrogenase from Arthrobacter sp. Strain 1C Isolation of (1-d-Carboxyethyl)-l-Phenylalanine-Assimilating Bacteria Purification of Opine Dehydrogenase from Arthrobacter sp. Strain 1C Cloning, Nucleotide Sequencing, and Expression of Opine Dehydrogenase Stereoselective Synthesis of Opine-Type Secondary Amine Carboxylic Acids by Opine Dehydrogenase Conclusion Bibliography Keywords: amino acid dehydrogenase; enzymatic synthesis; enzyme purification and properties; Opine compound; Opine dehydrogenase; secondary amine dicarboxylic acid
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Encyclopedia of Industrial Biotechnology - Opine Dehydrogenase, Secondary Amine Dicarboxylic Acids
Encyclopedia of Industrial Biotechnology, 2010Co-Authors: Yasuo Kato, Yasuhisa AsanoAbstract:Naturally Occurring Opines Secondary Amine Dicarboxylic Acids Enzymes Acting on Secondary Amine Dicarboxylic Acids Opine Dehydrogenase from Arthrobacter sp. Strain 1C Isolation of (1-d-Carboxyethyl)-l-Phenylalanine-Assimilating Bacteria Purification of Opine Dehydrogenase from Arthrobacter sp. Strain 1C Cloning, Nucleotide Sequencing, and Expression of Opine Dehydrogenase Stereoselective Synthesis of Opine-Type Secondary Amine Carboxylic Acids by Opine Dehydrogenase Conclusion References Keywords: amino acid dehydrogenase; enzymatic synthesis; enzyme purification and properties; Opine compound; Opine dehydrogenase; secondary amine dicarboxylic acid
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stereoselective synthesis of Opine type secondary amine car ylic acids by a new enzyme Opine dehydrogenase use of recombinant enzymes
Journal of Molecular Catalysis B-enzymatic, 1996Co-Authors: Yasuo Kato, Hideaki Yamada, Yasuhisa AsanoAbstract:Abstract The substrate specificity of the recently discovered enzyme, Opine dehydrogenase (ODH) fromArthrobacter sp. strain 1C for amino donors in the reaction that forms secondary amines using pyruvate as a fixed amino acceptor is examined. The enzyme was active toward short-chain aliphatic (S)-amino acids and those substituted with acyloxy, phosphonooxy, and halogen groups. The enzyme was named N-[1-(R)-(car☐yl)ethyl]-(S)-norvaline: NAD+ oxidoreductase (L-norvaline forming). Other substrates for the enzyme were 3-aminobutyric acid and (S)-phenylalaninol. Optically pure Opine-type secondary amine car☐ylic acids were synthesized from amino acids and their analogs such as (S)-methionine, (S)-isoleucine, (S)-leucine, (S)-valine, (S)-phenylalanine, (S)-alanine, (S)-threonine, (S)-serine, and (S)-phenylalaninol, and α-keto acids such as glyoxylate, pyruvate, and 2-oxobutyrate using the enzyme, with regeneration of NADH by formate dehydrogenase (FDH) fromMoraxella sp. C-1. The absolute configuration of the nascent asymmetric center of the Opines was of the (R) stereochemistry with > 99.9% e.e. One-pot synthesis of N-[1-(R)-(car☐yl)ethyl]-(S)-phenylalanine from phenylpyruvate and pyruvate by using ODH, FDH, and phenylalanine dehydrogenase (PheDH) fromBacillus sphaericus, is also described.
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Stereoselective synthesis of Opine-type secondary amine car☐ylic acids by a new enzyme Opine dehydrogenase use of recombinant enzymes
Journal of Molecular Catalysis B-enzymatic, 1996Co-Authors: Yasuo Kato, Hideaki Yamada, Yasuhisa AsanoAbstract:Abstract The substrate specificity of the recently discovered enzyme, Opine dehydrogenase (ODH) fromArthrobacter sp. strain 1C for amino donors in the reaction that forms secondary amines using pyruvate as a fixed amino acceptor is examined. The enzyme was active toward short-chain aliphatic (S)-amino acids and those substituted with acyloxy, phosphonooxy, and halogen groups. The enzyme was named N-[1-(R)-(car☐yl)ethyl]-(S)-norvaline: NAD+ oxidoreductase (L-norvaline forming). Other substrates for the enzyme were 3-aminobutyric acid and (S)-phenylalaninol. Optically pure Opine-type secondary amine car☐ylic acids were synthesized from amino acids and their analogs such as (S)-methionine, (S)-isoleucine, (S)-leucine, (S)-valine, (S)-phenylalanine, (S)-alanine, (S)-threonine, (S)-serine, and (S)-phenylalaninol, and α-keto acids such as glyoxylate, pyruvate, and 2-oxobutyrate using the enzyme, with regeneration of NADH by formate dehydrogenase (FDH) fromMoraxella sp. C-1. The absolute configuration of the nascent asymmetric center of the Opines was of the (R) stereochemistry with > 99.9% e.e. One-pot synthesis of N-[1-(R)-(car☐yl)ethyl]-(S)-phenylalanine from phenylpyruvate and pyruvate by using ODH, FDH, and phenylalanine dehydrogenase (PheDH) fromBacillus sphaericus, is also described.
Hideaki Yamada - One of the best experts on this subject based on the ideXlab platform.
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stereoselective synthesis of Opine type secondary amine car ylic acids by a new enzyme Opine dehydrogenase use of recombinant enzymes
Journal of Molecular Catalysis B-enzymatic, 1996Co-Authors: Yasuo Kato, Hideaki Yamada, Yasuhisa AsanoAbstract:Abstract The substrate specificity of the recently discovered enzyme, Opine dehydrogenase (ODH) fromArthrobacter sp. strain 1C for amino donors in the reaction that forms secondary amines using pyruvate as a fixed amino acceptor is examined. The enzyme was active toward short-chain aliphatic (S)-amino acids and those substituted with acyloxy, phosphonooxy, and halogen groups. The enzyme was named N-[1-(R)-(car☐yl)ethyl]-(S)-norvaline: NAD+ oxidoreductase (L-norvaline forming). Other substrates for the enzyme were 3-aminobutyric acid and (S)-phenylalaninol. Optically pure Opine-type secondary amine car☐ylic acids were synthesized from amino acids and their analogs such as (S)-methionine, (S)-isoleucine, (S)-leucine, (S)-valine, (S)-phenylalanine, (S)-alanine, (S)-threonine, (S)-serine, and (S)-phenylalaninol, and α-keto acids such as glyoxylate, pyruvate, and 2-oxobutyrate using the enzyme, with regeneration of NADH by formate dehydrogenase (FDH) fromMoraxella sp. C-1. The absolute configuration of the nascent asymmetric center of the Opines was of the (R) stereochemistry with > 99.9% e.e. One-pot synthesis of N-[1-(R)-(car☐yl)ethyl]-(S)-phenylalanine from phenylpyruvate and pyruvate by using ODH, FDH, and phenylalanine dehydrogenase (PheDH) fromBacillus sphaericus, is also described.
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Stereoselective synthesis of Opine-type secondary amine car☐ylic acids by a new enzyme Opine dehydrogenase use of recombinant enzymes
Journal of Molecular Catalysis B-enzymatic, 1996Co-Authors: Yasuo Kato, Hideaki Yamada, Yasuhisa AsanoAbstract:Abstract The substrate specificity of the recently discovered enzyme, Opine dehydrogenase (ODH) fromArthrobacter sp. strain 1C for amino donors in the reaction that forms secondary amines using pyruvate as a fixed amino acceptor is examined. The enzyme was active toward short-chain aliphatic (S)-amino acids and those substituted with acyloxy, phosphonooxy, and halogen groups. The enzyme was named N-[1-(R)-(car☐yl)ethyl]-(S)-norvaline: NAD+ oxidoreductase (L-norvaline forming). Other substrates for the enzyme were 3-aminobutyric acid and (S)-phenylalaninol. Optically pure Opine-type secondary amine car☐ylic acids were synthesized from amino acids and their analogs such as (S)-methionine, (S)-isoleucine, (S)-leucine, (S)-valine, (S)-phenylalanine, (S)-alanine, (S)-threonine, (S)-serine, and (S)-phenylalaninol, and α-keto acids such as glyoxylate, pyruvate, and 2-oxobutyrate using the enzyme, with regeneration of NADH by formate dehydrogenase (FDH) fromMoraxella sp. C-1. The absolute configuration of the nascent asymmetric center of the Opines was of the (R) stereochemistry with > 99.9% e.e. One-pot synthesis of N-[1-(R)-(car☐yl)ethyl]-(S)-phenylalanine from phenylpyruvate and pyruvate by using ODH, FDH, and phenylalanine dehydrogenase (PheDH) fromBacillus sphaericus, is also described.