4.1.1.11 748086 An archaeal glutamate decarboxylase homolog functions as an aspartate decarboxylase and is involved in beta-alanine and coenzyme A biosynthesis J. Bacteriol. 196 1222-1230 2014 Thermococcus kodakarensis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=24415726&form=6&db=m 4.1.1.11 748086 An archaeal glutamate decarboxylase homolog functions as an aspartate decarboxylase and is involved in beta-alanine and coenzyme A biosynthesis J. Bacteriol. 196 1222-1230 2014 Thermococcus kodakarensis ATCC BAA-918 / JCM 12380 / KOD1 http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=24415726&form=6&db=m 4.1.1.11 749304 Aspartate decarboxylase is required for a normal pupa pigmentation pattern in the silkworm, Bombyx mori Sci. Rep. 5 10885 2015 Bombyx mori http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26077025&form=6&db=m 4.1.1.11 747593 Characterization of L-aspartate-alpha-decarboxylase from Bacillus subtilis Chin. J. Biotechnol. 31 1184-1193 2015 Escherichia coli http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26762040&form=6&db=m 4.1.1.11 747593 Characterization of L-aspartate-alpha-decarboxylase from Bacillus subtilis Chin. J. Biotechnol. 31 1184-1193 2015 Bacillus subtilis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26762040&form=6&db=m 4.1.1.11 747593 Characterization of L-aspartate-alpha-decarboxylase from Bacillus subtilis Chin. J. Biotechnol. 31 1184-1193 2015 Corynebacterium glutamicum http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26762040&form=6&db=m 4.1.1.11 747593 Characterization of L-aspartate-alpha-decarboxylase from Bacillus subtilis Chin. J. Biotechnol. 31 1184-1193 2015 Bacillus subtilis 168 http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26762040&form=6&db=m 4.1.1.11 747593 Characterization of L-aspartate-alpha-decarboxylase from Bacillus subtilis Chin. J. Biotechnol. 31 1184-1193 2015 Corynebacterium glutamicum DSM 20300 http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26762040&form=6&db=m 4.1.1.11 744560 Gene expression and characterization of thermostable glutamate decarboxylase from Pyrococcus furiosus Biotechnol. Bioprocess Eng. 18 375-381 2013 Pyrococcus furiosus - 4.1.1.11 749207 Glu56Ser mutation improves the enzymatic activity and catalytic stability of Bacillus subtilis L-aspartate alpha-decarboxylase for an efficient beta-alanine production Process Biochem. 70 117-123 2018 Escherichia coli - 4.1.1.11 749207 Glu56Ser mutation improves the enzymatic activity and catalytic stability of Bacillus subtilis L-aspartate alpha-decarboxylase for an efficient beta-alanine production Process Biochem. 70 117-123 2018 Bacillus subtilis - 4.1.1.11 749207 Glu56Ser mutation improves the enzymatic activity and catalytic stability of Bacillus subtilis L-aspartate alpha-decarboxylase for an efficient beta-alanine production Process Biochem. 70 117-123 2018 Lactiplantibacillus plantarum - 4.1.1.11 749207 Glu56Ser mutation improves the enzymatic activity and catalytic stability of Bacillus subtilis L-aspartate alpha-decarboxylase for an efficient beta-alanine production Process Biochem. 70 117-123 2018 Corynebacterium glutamicum - 4.1.1.11 749207 Glu56Ser mutation improves the enzymatic activity and catalytic stability of Bacillus subtilis L-aspartate alpha-decarboxylase for an efficient beta-alanine production Process Biochem. 70 117-123 2018 Bacillus subtilis 168 - 4.1.1.11 749207 Glu56Ser mutation improves the enzymatic activity and catalytic stability of Bacillus subtilis L-aspartate alpha-decarboxylase for an efficient beta-alanine production Process Biochem. 70 117-123 2018 Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 - 4.1.1.11 749207 Glu56Ser mutation improves the enzymatic activity and catalytic stability of Bacillus subtilis L-aspartate alpha-decarboxylase for an efficient beta-alanine production Process Biochem. 70 117-123 2018 Lactiplantibacillus plantarum ATCC BAA-793 / NCIMB 8826 / WCFS1 - 4.1.1.11 746598 In vivo-selected pyrazinoic acid-resistant Mycobacterium tuberculosis strains harbor missense mutations in the aspartate decarboxylase PanD and the unfoldase ClpC1 ACS Infect. Dis. 3 492-501 2017 Mycobacterium tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28271875&form=6&db=m 4.1.1.11 746859 Molecular engineering of L-aspartate-alpha-decarboxylase for improved activity and catalytic stability Appl. Microbiol. Biotechnol. 101 6015-6021 2017 Escherichia coli http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28589224&form=6&db=m 4.1.1.11 746859 Molecular engineering of L-aspartate-alpha-decarboxylase for improved activity and catalytic stability Appl. Microbiol. Biotechnol. 101 6015-6021 2017 Bacillus subtilis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28589224&form=6&db=m 4.1.1.11 746859 Molecular engineering of L-aspartate-alpha-decarboxylase for improved activity and catalytic stability Appl. Microbiol. Biotechnol. 101 6015-6021 2017 Corynebacterium glutamicum http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28589224&form=6&db=m 4.1.1.11 746859 Molecular engineering of L-aspartate-alpha-decarboxylase for improved activity and catalytic stability Appl. Microbiol. Biotechnol. 101 6015-6021 2017 Bacillus subtilis 168 http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28589224&form=6&db=m 4.1.1.11 746859 Molecular engineering of L-aspartate-alpha-decarboxylase for improved activity and catalytic stability Appl. Microbiol. Biotechnol. 101 6015-6021 2017 Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28589224&form=6&db=m 4.1.1.11 746859 Molecular engineering of L-aspartate-alpha-decarboxylase for improved activity and catalytic stability Appl. Microbiol. Biotechnol. 101 6015-6021 2017 Escherichia coli K-12 / DH5alpha http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28589224&form=6&db=m 4.1.1.11 747799 Pantothenate auxotrophy in Zymomonas mobilis ZM4 is due to a lack of aspartate decarboxylase activity FEMS Microbiol. Lett. 364 fnx113 2017 no activity in Zymomonas mobilis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28655181&form=6&db=m 4.1.1.11 747799 Pantothenate auxotrophy in Zymomonas mobilis ZM4 is due to a lack of aspartate decarboxylase activity FEMS Microbiol. Lett. 364 fnx113 2017 Escherichia coli http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28655181&form=6&db=m 4.1.1.11 747799 Pantothenate auxotrophy in Zymomonas mobilis ZM4 is due to a lack of aspartate decarboxylase activity FEMS Microbiol. Lett. 364 fnx113 2017 no activity in Zymomonas mobilis ZM4 / ATCC 31821 / CP4 http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28655181&form=6&db=m 4.1.1.11 747435 Phylogenetic and amino acid conservation analyses of bacterial L-aspartate-alpha-decarboxylase and of its zymogen-maturation protein reveal a putative interaction domain BMC Res. Notes 8 354 2015 Halalkalibacterium halodurans http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26276430&form=6&db=m 4.1.1.11 747435 Phylogenetic and amino acid conservation analyses of bacterial L-aspartate-alpha-decarboxylase and of its zymogen-maturation protein reveal a putative interaction domain BMC Res. Notes 8 354 2015 Legionella pneumophila http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26276430&form=6&db=m 4.1.1.11 747435 Phylogenetic and amino acid conservation analyses of bacterial L-aspartate-alpha-decarboxylase and of its zymogen-maturation protein reveal a putative interaction domain BMC Res. Notes 8 354 2015 Klebsiella pneumoniae http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26276430&form=6&db=m 4.1.1.11 747435 Phylogenetic and amino acid conservation analyses of bacterial L-aspartate-alpha-decarboxylase and of its zymogen-maturation protein reveal a putative interaction domain BMC Res. Notes 8 354 2015 Helicobacter pylori http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26276430&form=6&db=m 4.1.1.11 747435 Phylogenetic and amino acid conservation analyses of bacterial L-aspartate-alpha-decarboxylase and of its zymogen-maturation protein reveal a putative interaction domain BMC Res. Notes 8 354 2015 Salmonella enterica subsp. enterica serovar Typhimurium http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26276430&form=6&db=m 4.1.1.11 747435 Phylogenetic and amino acid conservation analyses of bacterial L-aspartate-alpha-decarboxylase and of its zymogen-maturation protein reveal a putative interaction domain BMC Res. Notes 8 354 2015 Moorella thermoacetica http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26276430&form=6&db=m 4.1.1.11 747435 Phylogenetic and amino acid conservation analyses of bacterial L-aspartate-alpha-decarboxylase and of its zymogen-maturation protein reveal a putative interaction domain BMC Res. Notes 8 354 2015 Magnetospirillum magneticum http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26276430&form=6&db=m 4.1.1.11 747435 Phylogenetic and amino acid conservation analyses of bacterial L-aspartate-alpha-decarboxylase and of its zymogen-maturation protein reveal a putative interaction domain BMC Res. Notes 8 354 2015 Neisseria gonorrhoeae http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26276430&form=6&db=m 4.1.1.11 747435 Phylogenetic and amino acid conservation analyses of bacterial L-aspartate-alpha-decarboxylase and of its zymogen-maturation protein reveal a putative interaction domain BMC Res. Notes 8 354 2015 Bordetella pertussis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26276430&form=6&db=m 4.1.1.11 747435 Phylogenetic and amino acid conservation analyses of bacterial L-aspartate-alpha-decarboxylase and of its zymogen-maturation protein reveal a putative interaction domain BMC Res. Notes 8 354 2015 Ralstonia solanacearum http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26276430&form=6&db=m 4.1.1.11 747435 Phylogenetic and amino acid conservation analyses of bacterial L-aspartate-alpha-decarboxylase and of its zymogen-maturation protein reveal a putative interaction domain BMC Res. Notes 8 354 2015 Pseudomonas aeruginosa http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26276430&form=6&db=m 4.1.1.11 747435 Phylogenetic and amino acid conservation analyses of bacterial L-aspartate-alpha-decarboxylase and of its zymogen-maturation protein reveal a putative interaction domain BMC Res. Notes 8 354 2015 Corynebacterium glutamicum http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26276430&form=6&db=m 4.1.1.11 747435 Phylogenetic and amino acid conservation analyses of bacterial L-aspartate-alpha-decarboxylase and of its zymogen-maturation protein reveal a putative interaction domain BMC Res. Notes 8 354 2015 Neisseria gonorrhoeae ATCC 700825 / FA 1090 http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26276430&form=6&db=m 4.1.1.11 747435 Phylogenetic and amino acid conservation analyses of bacterial L-aspartate-alpha-decarboxylase and of its zymogen-maturation protein reveal a putative interaction domain BMC Res. Notes 8 354 2015 Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26276430&form=6&db=m 4.1.1.11 747435 Phylogenetic and amino acid conservation analyses of bacterial L-aspartate-alpha-decarboxylase and of its zymogen-maturation protein reveal a putative interaction domain BMC Res. Notes 8 354 2015 Magnetospirillum magneticum AMB-1 / ATCC 700264 http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26276430&form=6&db=m 4.1.1.11 747435 Phylogenetic and amino acid conservation analyses of bacterial L-aspartate-alpha-decarboxylase and of its zymogen-maturation protein reveal a putative interaction domain BMC Res. Notes 8 354 2015 Helicobacter pylori 26695 http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26276430&form=6&db=m 4.1.1.11 747435 Phylogenetic and amino acid conservation analyses of bacterial L-aspartate-alpha-decarboxylase and of its zymogen-maturation protein reveal a putative interaction domain BMC Res. Notes 8 354 2015 Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1 http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26276430&form=6&db=m 4.1.1.11 747435 Phylogenetic and amino acid conservation analyses of bacterial L-aspartate-alpha-decarboxylase and of its zymogen-maturation protein reveal a putative interaction domain BMC Res. Notes 8 354 2015 Salmonella enterica subsp. enterica serovar Typhimurium LT2 / SGSC1412 / ATCC 700720 http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26276430&form=6&db=m 4.1.1.11 747435 Phylogenetic and amino acid conservation analyses of bacterial L-aspartate-alpha-decarboxylase and of its zymogen-maturation protein reveal a putative interaction domain BMC Res. Notes 8 354 2015 Halalkalibacterium halodurans ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125 http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26276430&form=6&db=m 4.1.1.11 747435 Phylogenetic and amino acid conservation analyses of bacterial L-aspartate-alpha-decarboxylase and of its zymogen-maturation protein reveal a putative interaction domain BMC Res. Notes 8 354 2015 Klebsiella pneumoniae ATCC 700721 / MGH 78578 http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26276430&form=6&db=m 4.1.1.11 747435 Phylogenetic and amino acid conservation analyses of bacterial L-aspartate-alpha-decarboxylase and of its zymogen-maturation protein reveal a putative interaction domain BMC Res. Notes 8 354 2015 Moorella thermoacetica ATCC 39073 / JCM 9320 http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26276430&form=6&db=m 4.1.1.11 747435 Phylogenetic and amino acid conservation analyses of bacterial L-aspartate-alpha-decarboxylase and of its zymogen-maturation protein reveal a putative interaction domain BMC Res. Notes 8 354 2015 Bordetella pertussis Tohama I / ATCC BAA-589 / NCTC 13251 http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26276430&form=6&db=m 4.1.1.11 747380 Synthesis of beta-alanine from L-aspartate using L-aspartate-alpha-decarboxylase from Corynebacterium glutamicum Biotechnol. Lett. 36 1681-1686 2014 Corynebacterium glutamicum http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=24737081&form=6&db=m 4.1.1.11 747380 Synthesis of beta-alanine from L-aspartate using L-aspartate-alpha-decarboxylase from Corynebacterium glutamicum Biotechnol. Lett. 36 1681-1686 2014 Corynebacterium glutamicum ATCC 13032 http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=24737081&form=6&db=m 4.1.1.11 747128 The mechanism of regulation of pantothenate biosynthesis by the PanD-PanZ-AcCoA complex reveals an additional mode of action for the antimetabolite N-pentyl pantothenamide (N5-Pan) Biochemistry 56 4931-4939 2017 Escherichia coli http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28832133&form=6&db=m 4.1.1.11 747497 The structure of the PanD/PanZ protein complex reveals negative feedback regulation of pantothenate biosynthesis by coenzyme A Chem. 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