5.1.1.15 D-2-amino-delta-valerolactam best substrate Ensifer sp. 23-3 L-2-amino-delta-valerolactam - r 445375 5.1.1.15 D-2-amino-omega-octalactam 1.78% activity compared to D-2-aminohexano-6-lactam Ensifer sp. 23-3 L-2-amino-omega-octalactam - r 445376 5.1.1.15 D-2-aminobutyric acid amide 0.19% activity compared to D-2-aminohexano-6-lactam Ensifer sp. 23-3 L-2-aminobutyric acid amide - r 445377 5.1.1.15 D-2-aminohexano-6-lactam - Brucella anthropi L-2-aminohexano-6-lactam - r 444291 5.1.1.15 D-2-aminohexano-6-lactam - Glutamicibacter nicotianae L-2-aminohexano-6-lactam - r 444291 5.1.1.15 D-2-aminohexano-6-lactam - Achromobacter obae L-2-aminohexano-6-lactam - r 444291 5.1.1.15 D-2-aminohexano-6-lactam - Sinorhizobium medicae L-2-aminohexano-6-lactam - r 444291 5.1.1.15 D-2-aminohexano-6-lactam - Sinorhizobium meliloti L-2-aminohexano-6-lactam - r 444291 5.1.1.15 D-2-aminohexano-6-lactam - Janibacter sp. HTCC2649 L-2-aminohexano-6-lactam - r 444291 5.1.1.15 D-2-aminohexano-6-lactam - Mesorhizobium opportunistum L-2-aminohexano-6-lactam - r 444291 5.1.1.15 D-2-aminohexano-6-lactam - Mycolicibacterium vanbaalenii L-2-aminohexano-6-lactam - r 444291 5.1.1.15 D-2-aminohexano-6-lactam - Citreicella sp. SE45 L-2-aminohexano-6-lactam - r 444291 5.1.1.15 D-2-aminohexano-6-lactam - Ensifer sp. 23-3 L-2-aminohexano-6-lactam - r 444291 5.1.1.15 D-2-aminohexano-6-lactam preferred substrate Achromobacter obae L-2-aminohexano-6-lactam - r 444291 5.1.1.15 D-2-aminohexano-6-lactam preferred substrate Citreicella sp. SE45 L-2-aminohexano-6-lactam - r 444291 5.1.1.15 D-2-aminohexano-6-lactam high activity Ensifer sp. 23-3 L-2-aminohexano-6-lactam - r 444291 5.1.1.15 D-2-aminohexano-6-lactam - Brucella anthropi IA / NCBIMB41129 L-2-aminohexano-6-lactam - r 444291 5.1.1.15 D-Ala - Achromobacter obae L-Ala - r 884 5.1.1.15 D-alanine amide 2.12% activity compared to D-2-aminohexano-6-lactam Ensifer sp. 23-3 L-alanine amide - r 445384 5.1.1.15 D-alpha-amino-beta-caprolactam - Achromobacter obae DL-alpha-amino-beta-caprolactam - ? 376597 5.1.1.15 L-2-amino-delta-valerolactam 17.2% activity compared to D-2-aminohexano-6-lactam Ensifer sp. 23-3 D-2-amino-delta-valerolactam - r 445585 5.1.1.15 L-2-amino-omega-octalactam 1.41% activity compared to D-2-aminohexano-6-lactam Ensifer sp. 23-3 D-2-amino-omega-octalactam - r 445586 5.1.1.15 L-2-aminobutyric acid amide - Achromobacter obae D-2-aminobutyric acid amide - r 379972 5.1.1.15 L-2-aminobutyric acid amide 0.08% activity compared to D-2-aminohexano-6-lactam Ensifer sp. 23-3 D-2-aminobutyric acid amide - r 379972 5.1.1.15 L-2-aminohexano-6-lactam - Brucella anthropi D-2-aminohexano-6-lactam - r 444348 5.1.1.15 L-2-aminohexano-6-lactam - Glutamicibacter nicotianae D-2-aminohexano-6-lactam - r 444348 5.1.1.15 L-2-aminohexano-6-lactam - Achromobacter obae D-2-aminohexano-6-lactam - r 444348 5.1.1.15 L-2-aminohexano-6-lactam - Sinorhizobium medicae D-2-aminohexano-6-lactam - r 444348 5.1.1.15 L-2-aminohexano-6-lactam - Sinorhizobium meliloti D-2-aminohexano-6-lactam - r 444348 5.1.1.15 L-2-aminohexano-6-lactam - Janibacter sp. HTCC2649 D-2-aminohexano-6-lactam - r 444348 5.1.1.15 L-2-aminohexano-6-lactam - Mesorhizobium opportunistum D-2-aminohexano-6-lactam - r 444348 5.1.1.15 L-2-aminohexano-6-lactam - Mycolicibacterium vanbaalenii D-2-aminohexano-6-lactam - r 444348 5.1.1.15 L-2-aminohexano-6-lactam - Citreicella sp. SE45 D-2-aminohexano-6-lactam - r 444348 5.1.1.15 L-2-aminohexano-6-lactam high activity Achromobacter obae D-2-aminohexano-6-lactam - r 444348 5.1.1.15 L-2-aminohexano-6-lactam high activity Citreicella sp. SE45 D-2-aminohexano-6-lactam - r 444348 5.1.1.15 L-2-aminohexano-6-lactam high activity Ensifer sp. 23-3 D-2-aminohexano-6-lactam - r 444348 5.1.1.15 L-2-aminohexano-6-lactam - Brucella anthropi IA / NCBIMB41129 D-2-aminohexano-6-lactam - r 444348 5.1.1.15 L-alanine amide - Achromobacter obae D-alanine amide - ? 388969 5.1.1.15 L-alanine amide - Achromobacter obae D-alanine amide - r 388969 5.1.1.15 L-alanine amide - Citreicella sp. SE45 D-alanine amide - r 388969 5.1.1.15 L-alanine amide 0.77% activity compared to D-2-aminohexano-6-lactam Ensifer sp. 23-3 D-alanine amide - r 388969 5.1.1.15 L-alpha-Amino-beta-thio-epsilon-caprolactam racemized more than 3times faster and binds about 4fold stronger to the enzyme than L-alpha-amino-epsilon-caprolactam Achromobacter obae D-alpha-Amino-beta-thio-epsilon-caprolactam - ? 868 5.1.1.15 L-alpha-Amino-delta-valerolactam - Achromobacter obae D-alpha-Amino-delta-valerolactam - ? 869 5.1.1.15 L-alpha-Amino-epsilon-caprolactam - Pseudomonas sp. D-alpha-Amino-epsilon-caprolactam - ? 867 5.1.1.15 L-alpha-Amino-epsilon-caprolactam - Achromobacter obae D-alpha-Amino-epsilon-caprolactam - ? 867 5.1.1.15 L-alpha-Amino-epsilon-caprolactam - Achromobacter obae D-alpha-Amino-epsilon-caprolactam - r 867 5.1.1.15 L-alpha-Amino-epsilon-caprolactam r Achromobacter obae D-alpha-Amino-epsilon-caprolactam - ? 867 5.1.1.15 L-alpha-Amino-epsilon-caprolactam - Pseudomonas sp. CCM 3443 D-alpha-Amino-epsilon-caprolactam - ? 867 5.1.1.15 L-alpha-Amino-epsilon-caprolactam r Achromobacter obae FERM-P776 D-alpha-Amino-epsilon-caprolactam - ? 867 5.1.1.15 L-leucine amide - Achromobacter obae D-leucine amide - r 445613 5.1.1.15 L-leucine amide - Citreicella sp. SE45 D-leucine amide - r 445613 5.1.1.15 L-methionine amide - Achromobacter obae D-methionine amide - r 445616 5.1.1.15 L-methionine amide - Citreicella sp. SE45 D-methionine amide - r 445616 5.1.1.15 L-phenylalanine amide - Achromobacter obae D-phenylalanine amide - r 445623 5.1.1.15 L-phenylalanine amide - Citreicella sp. SE45 D-phenylalanine amide - r 445623 5.1.1.15 L-phenylglycine amide - Achromobacter obae D-phenylglycine amide - r 445626 5.1.1.15 L-phenylglycine amide - Citreicella sp. SE45 D-phenylglycine amide - r 445626 5.1.1.15 L-serine amide - Achromobacter obae D-serine amide - r 445648 5.1.1.15 L-serine amide - Citreicella sp. SE45 D-serine amide - r 445648 5.1.1.15 L-valine amide - Achromobacter obae D-valine amide - r 445682 5.1.1.15 L-valine amide - Citreicella sp. SE45 D-valine amide - r 445682 5.1.1.15 additional information the enzyme catalyzes alpha-proton exchange of the substrate with deuterium during racemization in deuterium oxide Achromobacter obae ? - ? 89 5.1.1.15 additional information no racemization activity is observed with dipeptides or amino acid derivatives, such as L-Ala-D-Ala, D-Ala-L-Ala, L-alanylglycine, L-phenylglycine, or L-alanine methylester Achromobacter obae ? - ? 89 5.1.1.15 additional information the enzyme encoded by gene ABI14443 is an amino acid amide racemase (UniProt ID Q06K28), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams Brucella anthropi ? - ? 89 5.1.1.15 additional information the enzyme encoded by gene CQ758817 shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams Glutamicibacter nicotianae ? - ? 89 5.1.1.15 additional information the enzyme encoded by gene CSE45_2055 is a 2,2-dialkylglycine decarboxylase, EC 4.1.1.64 (UniProt ID D0D2T1), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams Citreicella sp. SE45 ? - ? 89 5.1.1.15 additional information the enzyme encoded by gene JNB_04915 is a Putative aminotransferase protein (UniProt ID A3TM80), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams Janibacter sp. HTCC2649 ? - ? 89 5.1.1.15 additional information the enzyme encoded by gene Mesop_2670 is an aminotransferase class-III (UniProt ID F7Y223), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams Mesorhizobium opportunistum ? - ? 89 5.1.1.15 additional information the enzyme encoded by gene Mvan_2918 is an aminotransferase (EC 2.6.1, UniProt ID A1T974), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams Mycolicibacterium vanbaalenii ? - ? 89 5.1.1.15 additional information the enzyme encoded by gene Oant_4493 is an aminotransferase class-III (UniProt ID A6X7I5), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams Brucella anthropi ? - ? 89 5.1.1.15 additional information the enzyme encoded by gene SM0020_01805 is an acetylornithine transaminase (UniProt ID H0FT96), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams Sinorhizobium meliloti ? - ? 89 5.1.1.15 additional information the enzyme encoded by gene SMc02413 is a class-III pyridoxal-phosphate-dependent aminotransferase family protein, UniProt ID Q92MM4,that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams Sinorhizobium meliloti ? - ? 89 5.1.1.15 additional information the enzyme encoded by gene Smed_5339 is an aminotransferase class-III (UniProt ID A6UKD1), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams Sinorhizobium medicae ? - ? 89 5.1.1.15 additional information the enzyme acts on 2-aminohexano-6-lactam and 2-amino acid amides, the enzyme prefers the D-enantiomers as substrates Ensifer sp. 23-3 ? - ? 89 5.1.1.15 additional information The enzyme acts on a broad range of amino acid amides, particularly unbranched amino acid amides including L-alanine amide and L-serine amide. No activity with L-tyrosine amide Achromobacter obae ? - ? 89 5.1.1.15 additional information The enzyme acts on a broad range of amino acid amides, particularly unbranched amino acid amides including L-alanine amide and L-serine amide. No activity with L-tyrosine amide Citreicella sp. SE45 ? - ? 89 5.1.1.15 additional information the enzyme is also active on L-alanine, L-alanine amide, L-serine amide, L-leucine amide, L-valine amide, L-methionine amide, L-phenylalanine amide, and L-phenylglycine amide, and not active on L-tyrosine amide, cf. EC 5.1.1.10 Citreicella sp. SE45 ? - ? 89 5.1.1.15 additional information the enzyme is also active on L-alanine, L-alanine amide, L-serine amide, L-leucine amide, L-valine amide, L-methionine amide, L-phenylalanine amide, L-phenylglycine amide, and L-tyrosine amide, cf. EC 5.1.1.10 Sinorhizobium meliloti ? - ? 89 5.1.1.15 additional information the enzyme is also active on L-alanine, L-alanine amide, L-serine amide, L-valine amide, L-methionine amide, L-phenylalanine amide, and L-phenylglycine amide, and not active on L-leucine amide, and L-tyrosine amide, cf. EC 5.1.1.10 Brucella anthropi ? - ? 89 5.1.1.15 additional information the enzyme is also active on L-alanine, L-alanine amide, L-serine amide, L-valine amide, L-methionine amide, L-phenylalanine amide, and L-phenylglycine amide, and not active on L-leucine amide, and L-tyrosine amide, cf. EC 5.1.1.10 Sinorhizobium meliloti ? - ? 89 5.1.1.15 additional information the enzyme is also active on L-alanine, L-alanine amide, L-serine amide, L-valine amide, L-methionine amide, L-phenylalanine amide, and L-phenylglycine amide, and not active on L-leucine amide, and L-tyrosine amide, cf. EC 5.1.1.10 Janibacter sp. HTCC2649 ? - ? 89 5.1.1.15 additional information the enzyme is also active on L-alanine, L-alanine amide, L-serine amide, L-valine amide, L-methionine amide, L-phenylalanine amide, L-leucine amide, and L-phenylglycine amide, and not active on L-tyrosine amide, cf. EC 5.1.1.10 Achromobacter obae ? - ? 89 5.1.1.15 additional information the enzyme is also active on L-alanine, L-alanine amide, L-serine amide, L-valine amide, L-methionine amide, L-phenylalanine amide, L-phenylglycine amide, L-leucine amide, and L-tyrosine amide, cf. EC 5.1.1.10 Glutamicibacter nicotianae ? - ? 89 5.1.1.15 additional information the enzyme is also active on L-alanine, L-alanine amide, L-serine amide, L-valine amide, L-methionine amide, L-phenylalanine amide, L-phenylglycine amide, L-leucine amide, and L-tyrosine amide, cf. EC 5.1.1.10 Mesorhizobium opportunistum ? - ? 89 5.1.1.15 additional information the enzyme is also active on L-alanine, L-alanine amide, L-serine amide, L-valine amide, L-methionine amide, L-phenylalanine amide, L-tyrosine amide, and L-phenylglycine amide, and not active on L-leucine amide, cf. EC 5.1.1.10 Sinorhizobium medicae ? - ? 89 5.1.1.15 additional information the enzyme is also active on L-alanine, L-alanine amide, L-serine amide, L-valine amide, L-methionine amide, L-phenylalanine amide, L-tyrosine amide, and L-phenylglycine amide, and not active on L-leucine amide, cf. EC 5.1.1.10 Brucella anthropi ? - ? 89 5.1.1.15 additional information the enzyme is also active on L-alanine, L-alanine amide, L-valine amide, L-methionine amide, L-phenylalanine amide, and L-phenylglycine amide, and not active on L-leucine amide, L-serine amide, and L-tyrosine amide, cf. EC 5.1.1.10 Mycolicibacterium vanbaalenii ? - ? 89 5.1.1.15 additional information the enzyme encoded by gene ABI14443 is an amino acid amide racemase (UniProt ID Q06K28), that shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams Brucella anthropi IA / NCBIMB41129 ? - ? 89 5.1.1.15 additional information the enzyme is also active on L-alanine, L-alanine amide, L-serine amide, L-valine amide, L-methionine amide, L-phenylalanine amide, and L-phenylglycine amide, and not active on L-leucine amide, and L-tyrosine amide, cf. EC 5.1.1.10 Brucella anthropi IA / NCBIMB41129 ? - ? 89