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Timothy R. Hoover - One of the best experts on this subject based on the ideXlab platform.
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Crystal Structure of d‑Ornithine/d‑Lysine Decarboxylase, a Stereoinverting Decarboxylase: Implications for Substrate Specificity and Stereospecificity of Fold III Decarboxylases
2019Co-Authors: Robert S. Phillips, Pafe Poteh, Donovan Krajcovic, Katherine A. Miller, Timothy R. HooverAbstract:A newly discovered Fold III pyridoxal 5′-phosphate (PLP)-dependent Decarboxylase, d-ornithine/Lysine Decarboxylase (DOKDC), catalyzes decarboxylation of d-Lysine and d-ornithine with inversion of stereochemistry. The X-ray crystal structure of DOKDC has been determined to 1.72 Å. DOKDC has a low level of sequence identity (
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stm2360 encodes a d ornithine d Lysine Decarboxylase in salmonella enterica serovar typhimurium
Archives of Biochemistry and Biophysics, 2017Co-Authors: Robert S. Phillips, Pafe Poteh, Katherine A. Miller, Timothy R. HooverAbstract:Abstract STM2360 is a gene located in a small operon of undetermined function in Salmonella enterica serovar Typhimurium LT2. The amino acid sequence of STM2360 shows significant similarity (∼30% identity) to diaminopimelate Decarboxylase (DapDC), a Fold III pyridoxal-5′-phosphate (PLP) dependent enzyme involved in l -Lysine biosynthesis. We have found that the protein coded by STM2360 has a previously undocumented catalytic activity, d -ornithine/ d -Lysine Decarboxylase (DOKDC). The reaction products, cadaverine and putrescine, respectively, were identified by NMR and mass spectrometry. The substrate specificity of DOKDC is d -Lysine > d -Ornithine. This is the first pyridoxal-5′-phosphate dependent Decarboxylase identified to act on d -amino acids. STM2358, located in the same operon, has ornithine racemase activity. This suggests that the physiological substrate of the Decarboxylase and the operon is ornithine. Homologs of STM2360 with high sequence identity (>80%) are found in other common enterobacteria, including species of Klebsiella, Citrobacter, Vibrio and Hafnia, as well as Clostridium in the Firmicutes, and Pseudomonas.
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STM2360 encodes a d-ornithine/d-Lysine Decarboxylase in Salmonella enterica serovar typhimurium.
Archives of biochemistry and biophysics, 2017Co-Authors: Robert S. Phillips, Pafe Poteh, Katherine A. Miller, Timothy R. HooverAbstract:Abstract STM2360 is a gene located in a small operon of undetermined function in Salmonella enterica serovar Typhimurium LT2. The amino acid sequence of STM2360 shows significant similarity (∼30% identity) to diaminopimelate Decarboxylase (DapDC), a Fold III pyridoxal-5′-phosphate (PLP) dependent enzyme involved in l -Lysine biosynthesis. We have found that the protein coded by STM2360 has a previously undocumented catalytic activity, d -ornithine/ d -Lysine Decarboxylase (DOKDC). The reaction products, cadaverine and putrescine, respectively, were identified by NMR and mass spectrometry. The substrate specificity of DOKDC is d -Lysine > d -Ornithine. This is the first pyridoxal-5′-phosphate dependent Decarboxylase identified to act on d -amino acids. STM2358, located in the same operon, has ornithine racemase activity. This suggests that the physiological substrate of the Decarboxylase and the operon is ornithine. Homologs of STM2360 with high sequence identity (>80%) are found in other common enterobacteria, including species of Klebsiella, Citrobacter, Vibrio and Hafnia, as well as Clostridium in the Firmicutes, and Pseudomonas.
Robert S. Phillips - One of the best experts on this subject based on the ideXlab platform.
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Crystal Structure of d‑Ornithine/d‑Lysine Decarboxylase, a Stereoinverting Decarboxylase: Implications for Substrate Specificity and Stereospecificity of Fold III Decarboxylases
2019Co-Authors: Robert S. Phillips, Pafe Poteh, Donovan Krajcovic, Katherine A. Miller, Timothy R. HooverAbstract:A newly discovered Fold III pyridoxal 5′-phosphate (PLP)-dependent Decarboxylase, d-ornithine/Lysine Decarboxylase (DOKDC), catalyzes decarboxylation of d-Lysine and d-ornithine with inversion of stereochemistry. The X-ray crystal structure of DOKDC has been determined to 1.72 Å. DOKDC has a low level of sequence identity (
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stm2360 encodes a d ornithine d Lysine Decarboxylase in salmonella enterica serovar typhimurium
Archives of Biochemistry and Biophysics, 2017Co-Authors: Robert S. Phillips, Pafe Poteh, Katherine A. Miller, Timothy R. HooverAbstract:Abstract STM2360 is a gene located in a small operon of undetermined function in Salmonella enterica serovar Typhimurium LT2. The amino acid sequence of STM2360 shows significant similarity (∼30% identity) to diaminopimelate Decarboxylase (DapDC), a Fold III pyridoxal-5′-phosphate (PLP) dependent enzyme involved in l -Lysine biosynthesis. We have found that the protein coded by STM2360 has a previously undocumented catalytic activity, d -ornithine/ d -Lysine Decarboxylase (DOKDC). The reaction products, cadaverine and putrescine, respectively, were identified by NMR and mass spectrometry. The substrate specificity of DOKDC is d -Lysine > d -Ornithine. This is the first pyridoxal-5′-phosphate dependent Decarboxylase identified to act on d -amino acids. STM2358, located in the same operon, has ornithine racemase activity. This suggests that the physiological substrate of the Decarboxylase and the operon is ornithine. Homologs of STM2360 with high sequence identity (>80%) are found in other common enterobacteria, including species of Klebsiella, Citrobacter, Vibrio and Hafnia, as well as Clostridium in the Firmicutes, and Pseudomonas.
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STM2360 encodes a d-ornithine/d-Lysine Decarboxylase in Salmonella enterica serovar typhimurium.
Archives of biochemistry and biophysics, 2017Co-Authors: Robert S. Phillips, Pafe Poteh, Katherine A. Miller, Timothy R. HooverAbstract:Abstract STM2360 is a gene located in a small operon of undetermined function in Salmonella enterica serovar Typhimurium LT2. The amino acid sequence of STM2360 shows significant similarity (∼30% identity) to diaminopimelate Decarboxylase (DapDC), a Fold III pyridoxal-5′-phosphate (PLP) dependent enzyme involved in l -Lysine biosynthesis. We have found that the protein coded by STM2360 has a previously undocumented catalytic activity, d -ornithine/ d -Lysine Decarboxylase (DOKDC). The reaction products, cadaverine and putrescine, respectively, were identified by NMR and mass spectrometry. The substrate specificity of DOKDC is d -Lysine > d -Ornithine. This is the first pyridoxal-5′-phosphate dependent Decarboxylase identified to act on d -amino acids. STM2358, located in the same operon, has ornithine racemase activity. This suggests that the physiological substrate of the Decarboxylase and the operon is ornithine. Homologs of STM2360 with high sequence identity (>80%) are found in other common enterobacteria, including species of Klebsiella, Citrobacter, Vibrio and Hafnia, as well as Clostridium in the Firmicutes, and Pseudomonas.
Hidemasa Izumiya - One of the best experts on this subject based on the ideXlab platform.
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Lysine Decarboxylase-negative Salmonella enterica serovar enteritidis: antibiotic susceptibility, phage and PFGE typing.
The Journal of veterinary medical science, 2007Co-Authors: Shogo Yamasaki, Haruo Watanabe, Hidemasa Izumiya, Kenshi Hara, Naoaki Misawa, Karoku Okamoto, Kozo TakaseAbstract:One hundred twenty Salmonella Enteritidis isolates collected from 1992 to 2005 in Nagasaki prefecture (65 isolates from 40 outbreak cases, 44 from sporadic diarrhea patients, and 11 from chicken-related products) were investigated by their antibiotic susceptibility profiles, phage typing, and pulsed-field gel electrophoresis (PFGE) typing. Out of them, 18 were identified as Lysine Decarboxylase (LDC)-negative isolates, and 15 showed resistance toward streptomycin. Based on the PFGE typing, the isolates were classified into five clusters by UPGMA clustering method. Three LDC-negative isolates belonged to cluster A and were of phage type (PT) 4 and isolated between 2000 and 2004. Other 15 LDC-negative isolates belonged to cluster E. They were PT1, reacted but did not conform (RDNC), or untypable and were isolated between 2001 and 2004. LDC-negative isolates of the cluster A differed from LDC-negative isolates of the cluster E in antibiotic susceptibility profiles, phage typing, and PFGE typing. LDC-negative isolates of the cluster E were isolated after 2001 in Nagasaki prefecture.
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Characterization of Lysine Decarboxylase-negative strains of Salmonella enterica serovar Enteritidis disseminated in Japan
FEMS immunology and medical microbiology, 2006Co-Authors: Masatomo Morita, Kadumi Mori, Kiyoshi Tominaga, Jun Terajima, Kenji Hirose, Haruo Watanabe, Hidemasa IzumiyaAbstract:Salmonella enterica serovar Enteritidis is one of the leading causes of food-borne diseases in Japan. Typically, Salmonella spp. test positive for Lysine-Decarboxylase. However, the number of isolates of serovar Enteritidis without Lysine-Decarboxylase activity increased in Japan in 2003. Among 109 strains from distinct outbreaks, 10 lacked Lysine-Decarboxylase activity. Nine of the ten Lysine-Decarboxylase-negative strains showed quite similar pulsed-field gel electrophoresis profiles. Their Lysine-Decarboxylase phenotype was recovered by introduction of the cadBA locus from an Lysine-Decarboxylase-positive strain. Although the cad loci of the Lysine-Decarboxylase-negative strains seemed to be intact without any insertion sequences, cadC , a positive regulator of cadBA , had a single-base deletion at the same position, the 973rd base (cytosine), in all the nine Lysine-Decarboxylase-negative strains, whereas the wild-type cadC gene has a 1542 bp coding region (514 amino acids). This deletion was expected to produce a truncated (338 amino acids) form of CadC due to a frameshift. Because CadC senses environmental cues such as external pH and Lysine through its putative C-terminal periplasmic domain, it is likely that the truncated CadC is not sensitive enough to external signaling to activate the cadBA operon, resulting in loss of the Lysine-Decarboxylase activity. Our results suggest that dissemination of these genetically closely related strains of serovar Enteritidis accounts for the unusual increase in the isolation of Lysine-Decarboxylase-negative strains.
Katherine A. Miller - One of the best experts on this subject based on the ideXlab platform.
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Crystal Structure of d‑Ornithine/d‑Lysine Decarboxylase, a Stereoinverting Decarboxylase: Implications for Substrate Specificity and Stereospecificity of Fold III Decarboxylases
2019Co-Authors: Robert S. Phillips, Pafe Poteh, Donovan Krajcovic, Katherine A. Miller, Timothy R. HooverAbstract:A newly discovered Fold III pyridoxal 5′-phosphate (PLP)-dependent Decarboxylase, d-ornithine/Lysine Decarboxylase (DOKDC), catalyzes decarboxylation of d-Lysine and d-ornithine with inversion of stereochemistry. The X-ray crystal structure of DOKDC has been determined to 1.72 Å. DOKDC has a low level of sequence identity (
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stm2360 encodes a d ornithine d Lysine Decarboxylase in salmonella enterica serovar typhimurium
Archives of Biochemistry and Biophysics, 2017Co-Authors: Robert S. Phillips, Pafe Poteh, Katherine A. Miller, Timothy R. HooverAbstract:Abstract STM2360 is a gene located in a small operon of undetermined function in Salmonella enterica serovar Typhimurium LT2. The amino acid sequence of STM2360 shows significant similarity (∼30% identity) to diaminopimelate Decarboxylase (DapDC), a Fold III pyridoxal-5′-phosphate (PLP) dependent enzyme involved in l -Lysine biosynthesis. We have found that the protein coded by STM2360 has a previously undocumented catalytic activity, d -ornithine/ d -Lysine Decarboxylase (DOKDC). The reaction products, cadaverine and putrescine, respectively, were identified by NMR and mass spectrometry. The substrate specificity of DOKDC is d -Lysine > d -Ornithine. This is the first pyridoxal-5′-phosphate dependent Decarboxylase identified to act on d -amino acids. STM2358, located in the same operon, has ornithine racemase activity. This suggests that the physiological substrate of the Decarboxylase and the operon is ornithine. Homologs of STM2360 with high sequence identity (>80%) are found in other common enterobacteria, including species of Klebsiella, Citrobacter, Vibrio and Hafnia, as well as Clostridium in the Firmicutes, and Pseudomonas.
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STM2360 encodes a d-ornithine/d-Lysine Decarboxylase in Salmonella enterica serovar typhimurium.
Archives of biochemistry and biophysics, 2017Co-Authors: Robert S. Phillips, Pafe Poteh, Katherine A. Miller, Timothy R. HooverAbstract:Abstract STM2360 is a gene located in a small operon of undetermined function in Salmonella enterica serovar Typhimurium LT2. The amino acid sequence of STM2360 shows significant similarity (∼30% identity) to diaminopimelate Decarboxylase (DapDC), a Fold III pyridoxal-5′-phosphate (PLP) dependent enzyme involved in l -Lysine biosynthesis. We have found that the protein coded by STM2360 has a previously undocumented catalytic activity, d -ornithine/ d -Lysine Decarboxylase (DOKDC). The reaction products, cadaverine and putrescine, respectively, were identified by NMR and mass spectrometry. The substrate specificity of DOKDC is d -Lysine > d -Ornithine. This is the first pyridoxal-5′-phosphate dependent Decarboxylase identified to act on d -amino acids. STM2358, located in the same operon, has ornithine racemase activity. This suggests that the physiological substrate of the Decarboxylase and the operon is ornithine. Homologs of STM2360 with high sequence identity (>80%) are found in other common enterobacteria, including species of Klebsiella, Citrobacter, Vibrio and Hafnia, as well as Clostridium in the Firmicutes, and Pseudomonas.
Pafe Poteh - One of the best experts on this subject based on the ideXlab platform.
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Crystal Structure of d‑Ornithine/d‑Lysine Decarboxylase, a Stereoinverting Decarboxylase: Implications for Substrate Specificity and Stereospecificity of Fold III Decarboxylases
2019Co-Authors: Robert S. Phillips, Pafe Poteh, Donovan Krajcovic, Katherine A. Miller, Timothy R. HooverAbstract:A newly discovered Fold III pyridoxal 5′-phosphate (PLP)-dependent Decarboxylase, d-ornithine/Lysine Decarboxylase (DOKDC), catalyzes decarboxylation of d-Lysine and d-ornithine with inversion of stereochemistry. The X-ray crystal structure of DOKDC has been determined to 1.72 Å. DOKDC has a low level of sequence identity (
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stm2360 encodes a d ornithine d Lysine Decarboxylase in salmonella enterica serovar typhimurium
Archives of Biochemistry and Biophysics, 2017Co-Authors: Robert S. Phillips, Pafe Poteh, Katherine A. Miller, Timothy R. HooverAbstract:Abstract STM2360 is a gene located in a small operon of undetermined function in Salmonella enterica serovar Typhimurium LT2. The amino acid sequence of STM2360 shows significant similarity (∼30% identity) to diaminopimelate Decarboxylase (DapDC), a Fold III pyridoxal-5′-phosphate (PLP) dependent enzyme involved in l -Lysine biosynthesis. We have found that the protein coded by STM2360 has a previously undocumented catalytic activity, d -ornithine/ d -Lysine Decarboxylase (DOKDC). The reaction products, cadaverine and putrescine, respectively, were identified by NMR and mass spectrometry. The substrate specificity of DOKDC is d -Lysine > d -Ornithine. This is the first pyridoxal-5′-phosphate dependent Decarboxylase identified to act on d -amino acids. STM2358, located in the same operon, has ornithine racemase activity. This suggests that the physiological substrate of the Decarboxylase and the operon is ornithine. Homologs of STM2360 with high sequence identity (>80%) are found in other common enterobacteria, including species of Klebsiella, Citrobacter, Vibrio and Hafnia, as well as Clostridium in the Firmicutes, and Pseudomonas.
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STM2360 encodes a d-ornithine/d-Lysine Decarboxylase in Salmonella enterica serovar typhimurium.
Archives of biochemistry and biophysics, 2017Co-Authors: Robert S. Phillips, Pafe Poteh, Katherine A. Miller, Timothy R. HooverAbstract:Abstract STM2360 is a gene located in a small operon of undetermined function in Salmonella enterica serovar Typhimurium LT2. The amino acid sequence of STM2360 shows significant similarity (∼30% identity) to diaminopimelate Decarboxylase (DapDC), a Fold III pyridoxal-5′-phosphate (PLP) dependent enzyme involved in l -Lysine biosynthesis. We have found that the protein coded by STM2360 has a previously undocumented catalytic activity, d -ornithine/ d -Lysine Decarboxylase (DOKDC). The reaction products, cadaverine and putrescine, respectively, were identified by NMR and mass spectrometry. The substrate specificity of DOKDC is d -Lysine > d -Ornithine. This is the first pyridoxal-5′-phosphate dependent Decarboxylase identified to act on d -amino acids. STM2358, located in the same operon, has ornithine racemase activity. This suggests that the physiological substrate of the Decarboxylase and the operon is ornithine. Homologs of STM2360 with high sequence identity (>80%) are found in other common enterobacteria, including species of Klebsiella, Citrobacter, Vibrio and Hafnia, as well as Clostridium in the Firmicutes, and Pseudomonas.
