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Amidohydrolases

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Liis Andresen – One of the best experts on this subject based on the ideXlab platform.

  • AepA of Pectobacterium is not involved in the regulation of extracellular plant cell wall degrading enzymes production
    Molecular Genetics and Genomics, 2010
    Co-Authors: Viia Koiv, Liis Andresen
    Abstract:

    Plant cell wall degrading enzymes (PCWDE) are the major virulence determinants in phytopathogenic Pectobacterium , and their production is controlled by many regulatory factors. In this study, we focus on the role of the AepA protein, which was previously described to be a global regulator of PCWDE production in Pectobacterium carotovorum (Murata et al. in Mol Plant Microbe Interact 4:239–246, 1991 ) . Our results show that neither inactivation nor overexpression of aepA affects PCWDE production in either Pectobacterium atrosepticum SCRI1043 or Pectobacterium carotovorum subsp. carotovorum SCC3193 . The previously published observation based on the overexpression of aepA could be explained by the presence of the adjacent regulatory rsmB gene in the constructs used. Our database searches indicated that AepA belongs to the YtcJ subfamily of Amidohydrolases. YtcJ-like Amidohydrolases are present in bacteria, archaea, plants and some fungi. Although AepA has 28% identity with the formamide deformylase NfdA in Arthrobacter pascens F164, AepA was unable to catalyze the degradation of NdfA-specific N-substituted formamides. We conclude that AepA is a putative aminohydrolase not involved in regulation of PCWDE production.

  • AepA of Pectobacterium is not involved in the regulation of extracellular plant cell wall degrading enzymes production
    Molecular Genetics and Genomics, 2010
    Co-Authors: Viia Koiv, Liis Andresen
    Abstract:

    Plant cell wall degrading enzymes (PCWDE) are the major virulence determinants in phytopathogenic Pectobacterium , and their production is controlled by many regulatory factors. In this study, we focus on the role of the AepA protein, which was previously described to be a global regulator of PCWDE production in Pectobacterium carotovorum (Murata et al. in Mol Plant Microbe Interact 4:239–246, 1991 ) . Our results show that neither inactivation nor overexpression of aepA affects PCWDE production in either Pectobacterium atrosepticum SCRI1043 or Pectobacterium carotovorum subsp. carotovorum SCC3193 . The previously published observation based on the overexpression of aepA could be explained by the presence of the adjacent regulatory rsmB gene in the constructs used. Our database searches indicated that AepA belongs to the YtcJ subfamily of Amidohydrolases. YtcJ-like Amidohydrolases are present in bacteria, archaea, plants and some fungi. Although AepA has 28% identity with the formamide deformylase NfdA in Arthrobacter pascens F164, AepA was unable to catalyze the degradation of NdfA-specific N-substituted formamides. We conclude that AepA is a putative aminohydrolase not involved in regulation of PCWDE production.

A M Edwards – One of the best experts on this subject based on the ideXlab platform.

  • the crystal structure of hypothetical protein mth1491 from methanobacterium thermoautotrophicum
    Protein Science, 2002
    Co-Authors: Dinesh Christendat, A M Edwards, V Saridakis, Ponni A Kumar, Xiaohui Xu, A Semesi, Andzrej Joachimiak, C H Arrowsmith
    Abstract:

    As part of our structural proteomics initiative, we have determined the crystal structure of MTH1491, a previously uncharacterized hypothetical protein from Methanobacterium thermoautotrophicum. MTH1491 is one of numerous structural genomics targets selected in a genome-wide survey of uncharacterized proteins. It belongs to a family of proteins whose biological function is not known. The crystal structure of MTH1491, the first structure for this family of proteins, consists of an overall five-stranded parallel β-sheet with strand order 51234 and flanking helices. The oligomeric form of this molecule is a trimer as seen from both crystal contacts and gel filtfiltration studies. Analysis revealed that the structure of MTH1491 is similar to that of dehydrogenases, Amidohydrolases, and oxidoreductases. Using a combination of sequence and structural analyses, we showed that MTH1491 does not belong to either the dehydrogenase or the amidohydrolase superfamilies of proteins.

  • the crystal structure of hypothetical protein mth1491 from methanobacterium thermoautotrophicum
    Protein Science, 2002
    Co-Authors: Dinesh Christendat, A M Edwards, V Saridakis, Ponni A Kumar, A Semesi, Andzrej Joachimiak, C H Arrowsmith, Youngchang Kim
    Abstract:

    As part of our structural proteomics initiative, we have determined the crystal structure of MTH1491, a previously uncharacterized hypothetical protein from Methanobacterium thermoautotrophicum. MTH1491 is one of numerous structural genomics targets selected in a genome-wide survey of uncharacterized proteins. It belongs to a family of proteins whose biological function is not known. The crystal structure of MTH1491, the first structure for this family of proteins, consists of an overall five-stranded parallel beta-sheet with strand order 51234 and flanking helices. The oligomeric form of this molecule is a trimer as seen from both crystal contacts and gel filtfiltration studies. Analysis revealed that the structure of MTH1491 is similar to that of dehydrogenases, Amidohydrolases, and oxidoreductases. Using a combination of sequence and structural analyses, we showed that MTH1491 does not belong to either the dehydrogenase or the amidohydrolase superfamilies of proteins.

Nadia Raffaelli – One of the best experts on this subject based on the ideXlab platform.

  • characterization of bacterial nmn deamidase as a ser lys hydrolase expands diversity of serine Amidohydrolases
    FEBS Letters, 2014
    Co-Authors: Leonardo Sorci, Lucia Brunetti, Lucia Cialabrini, Francesca Mazzola, Marat D. Kazanov, Silverio Ruggieri, Sabato Dauria, Nadia Raffaelli
    Abstract:

    NMN deamidase (PncC) is a bacterial enzyme involved in NAD biosynthesis. We have previously demonstrated that PncC is structurally distinct from other known Amidohydrolases. Here, we extended PncC characterization by mutating all potential catalytic residues and assessing their individual roles in catalysis through kinetic analyses. Inspection of these residues’ spatial arrangement in the active site, allowed us to conclude that PncC is a serine-amidohydrolase, employing a Ser/Lys dyad for catalysis. Analysis of the PncC structure in complex with a modeled NMN substrate supported our conclusion, and enabled us to propose the catalytic mechanism.

  • Characterization of bacterial NMN deamidase as a Ser/Lys hydrolase expands diversity of serine Amidohydrolases
    FEBS letters, 2014
    Co-Authors: Leonardo Sorci, Lucia Brunetti, Lucia Cialabrini, Francesca Mazzola, Marat D. Kazanov, Sabato D'auria, Silverio Ruggieri, Nadia Raffaelli
    Abstract:

    NMN deamidase (PncC) is a bacterial enzyme involved in NAD biosynthesis. We have previously demonstrated that PncC is structurally distinct from other known Amidohydrolases. Here, we extended PncC characterization by mutating all potential catalytic residues and assessing their individual roles in catalysis through kinetic analyses. Inspection of these residues’ spatial arrangement in the active site, allowed us to conclude that PncC is a serine-amidohydrolase, employing a Ser/Lys dyad for catalysis. Analysis of the PncC structure in complex with a modeled NMN substrate supported our conclusion, and enabled us to propose the catalytic mechanism.

Viia Koiv – One of the best experts on this subject based on the ideXlab platform.

  • AepA of Pectobacterium is not involved in the regulation of extracellular plant cell wall degrading enzymes production
    Molecular Genetics and Genomics, 2010
    Co-Authors: Viia Koiv, Liis Andresen
    Abstract:

    Plant cell wall degrading enzymes (PCWDE) are the major virulence determinants in phytopathogenic Pectobacterium , and their production is controlled by many regulatory factors. In this study, we focus on the role of the AepA protein, which was previously described to be a global regulator of PCWDE production in Pectobacterium carotovorum (Murata et al. in Mol Plant Microbe Interact 4:239–246, 1991 ) . Our results show that neither inactivation nor overexpression of aepA affects PCWDE production in either Pectobacterium atrosepticum SCRI1043 or Pectobacterium carotovorum subsp. carotovorum SCC3193 . The previously published observation based on the overexpression of aepA could be explained by the presence of the adjacent regulatory rsmB gene in the constructs used. Our database searches indicated that AepA belongs to the YtcJ subfamily of Amidohydrolases. YtcJ-like Amidohydrolases are present in bacteria, archaea, plants and some fungi. Although AepA has 28% identity with the formamide deformylase NfdA in Arthrobacter pascens F164, AepA was unable to catalyze the degradation of NdfA-specific N-substituted formamides. We conclude that AepA is a putative aminohydrolase not involved in regulation of PCWDE production.

  • AepA of Pectobacterium is not involved in the regulation of extracellular plant cell wall degrading enzymes production
    Molecular Genetics and Genomics, 2010
    Co-Authors: Viia Koiv, Liis Andresen
    Abstract:

    Plant cell wall degrading enzymes (PCWDE) are the major virulence determinants in phytopathogenic Pectobacterium , and their production is controlled by many regulatory factors. In this study, we focus on the role of the AepA protein, which was previously described to be a global regulator of PCWDE production in Pectobacterium carotovorum (Murata et al. in Mol Plant Microbe Interact 4:239–246, 1991 ) . Our results show that neither inactivation nor overexpression of aepA affects PCWDE production in either Pectobacterium atrosepticum SCRI1043 or Pectobacterium carotovorum subsp. carotovorum SCC3193 . The previously published observation based on the overexpression of aepA could be explained by the presence of the adjacent regulatory rsmB gene in the constructs used. Our database searches indicated that AepA belongs to the YtcJ subfamily of Amidohydrolases. YtcJ-like Amidohydrolases are present in bacteria, archaea, plants and some fungi. Although AepA has 28% identity with the formamide deformylase NfdA in Arthrobacter pascens F164, AepA was unable to catalyze the degradation of NdfA-specific N-substituted formamides. We conclude that AepA is a putative aminohydrolase not involved in regulation of PCWDE production.

Mitsuaki Moriguchi – One of the best experts on this subject based on the ideXlab platform.

  • Molecular chaperones facilitate the soluble expression of N-acyl-D-amino acid Amidohydrolases in Escherichia coli.
    Journal of industrial microbiology & biotechnology, 2004
    Co-Authors: Kazuaki Yoshimune, Mamoru Wakayama, Yoko Ninomiya, Mitsuaki Moriguchi
    Abstract:

    The overproduction of d-aminoacylase (d-ANase, 233.8 U/mg), N-acyl-d-glutamate amidohydrolase (d-AGase, 38.1 U/mg) or N-acyl-d-aspartate amidohydrolase (d-AAase, 6.2 U/mg) in Escherichia coli is accompanied by aggregation of the overproduced protein. To facilitate the expression of active enzymes, the molecular chaperones GroELGroES (GroELS), DnaK-DnaJ-GrpE (DnaKJE), trigger factor (TF), GroELS and DnaKJE or GroELS and TF were coexpressed with the enzymes. d-ANase (313.3 U/mg) and d-AGase (95.8 U/mg) were overproduced in an active form at levels 1.3- and 1.8-fold higher, respectively, upon co-expression of GroELS and TF. An E. coli strain expressing the d-AAase gene simultaneously with the TF gene exhibited a 4.3-fold enhancement in d-AAase activity (32.0 U/mg) compared with control E. coli expressing the d-AAase gene alone.

  • Production of d-amino acids by N-acyl-d-amino acid amidohydrolase and its structure and function
    Journal of Molecular Catalysis B-enzymatic, 2003
    Co-Authors: Mamoru Wakayama, Kazuaki Yoshimune, Yoshihiko Hirose, Mitsuaki Moriguchi
    Abstract:

    Abstract d –Amino acids have been widely used as synthetic materials for various compounds such as pharmaceuticals and agrochemicals. The manufacture of d –amino acids by fermentation is difficult, and enzymatic methods are mainly employed. At present, the optical resoresolution method using N-acyl- d –amino acid amidohydrolase is the most useful and convenient. In this review, the application of N-acyl- d –amino acid amidohydrolase to the production of d –amino acids and recent progress in the study of structure–function relationships from the standpoint of improving this enzyme for industrial application are discussed.

  • Comparative biochemistry of bacterial N-acyl-d-amino acid amidohydrolase
    Journal of Molecular Catalysis B-enzymatic, 2001
    Co-Authors: Mamoru Wakayama, Mitsuaki Moriguchi
    Abstract:

    Abstract N-acyl- d –amino acid Amidohydrolases can be classified into three types based on substrate specificity. d -aminoacylase has been reported to occur in a very few bacteria such as Pseudomonas, Streptomyces, and Alcaligenes. N-acyl- d -aspartate amidohydrolase ( d -AAase) has been reported in only Alcaligenes xylosoxydans subsp. xylosoxydans A-6 (Alcaligenes A-6) while N-acyl- d –glutamate amidohydrolase ( d -AGase) has been isolated in two stains of Pseudomonas sp. 5f-1 and Alcaligenes A-6. The physiological roles of these enzymes in these microbes are not clear. They are individually characteristic in their substrate specificities, inducer profiles, inhibitors, isoelectric points, metal dependency, and some physicochemical properties. The primary structures of all the three types of N-acyl- d –amino acid Amidohydrolases from Alcaligenes A-6 were determined from their nucleotide sequences. Comparison of their primary structures revealed high homology (46–56%) between the different enzymes. The three enzymes showed 26–27% sequence homology with l -aminoacylases from Bacillus steastearothermophilus, porcine, and human. Chemical modification and site-directed mutamutagenesis identified the histidyl residues essential for catalysis. The Alcaligenes N-acyl- d –amino acid Amidohydrolases share significant sequence similarities with some members of the urease-related amidohydrolase superfamily proposed by Holm and Sander [L. Holm, C. Sander, Proteins: Structure, Function and Genetics 28 (1997) 72].