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Literature summary extracted from
- In silico identification for alpha-amino-epsilon-caprolactam racemases by using information on the structure and function relationship (2015), Appl. Biochem. Biotechnol., 176, 1303-1314 .
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 5.1.1.10 | synthesis | the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production | Glutamicibacter nicotianae |
| 5.1.1.10 | synthesis | the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production | Achromobacter obae |
| 5.1.1.10 | synthesis | the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production | Sinorhizobium medicae |
| 5.1.1.10 | synthesis | the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production | Sinorhizobium meliloti |
| 5.1.1.10 | synthesis | the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production | Janibacter sp. HTCC2649 |
| 5.1.1.10 | synthesis | the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production | Mesorhizobium opportunistum |
| 5.1.1.10 | synthesis | the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production | Mycolicibacterium vanbaalenii |
| 5.1.1.10 | synthesis | the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production | Brucella anthropi |
| 5.1.1.10 | synthesis | the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production | Citreicella sp. SE45 |
| 5.1.1.15 | synthesis | the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production | Brucella anthropi |
| 5.1.1.15 | synthesis | the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production | Glutamicibacter nicotianae |
| 5.1.1.15 | synthesis | the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production | Achromobacter obae |
| 5.1.1.15 | synthesis | the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production | Sinorhizobium medicae |
| 5.1.1.15 | synthesis | the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production | Sinorhizobium meliloti |
| 5.1.1.15 | synthesis | the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production | Janibacter sp. HTCC2649 |
| 5.1.1.15 | synthesis | the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production | Mesorhizobium opportunistum |
| 5.1.1.15 | synthesis | the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production | Mycolicibacterium vanbaalenii |
| 5.1.1.15 | synthesis | the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production | Citreicella sp. SE45 |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.1.1.10 | gene ABI14443, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109 | Brucella anthropi |
| 5.1.1.10 | gene ACLR or Oant_4493, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109 | Brucella anthropi |
| 5.1.1.10 | gene ACLR or Smed_5339, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109 | Sinorhizobium medicae |
| 5.1.1.10 | gene ACLR, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109 | Achromobacter obae |
| 5.1.1.10 | gene CSE45_2055, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109 | Glutamicibacter nicotianae |
| 5.1.1.10 | gene CSE45_2055, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109 | Citreicella sp. SE45 |
| 5.1.1.10 | gene JNB_04915, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109 | Janibacter sp. HTCC2649 |
| 5.1.1.10 | gene Mesop_2670, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109 | Mesorhizobium opportunistum |
| 5.1.1.10 | gene Mvan_2918, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109 | Mycolicibacterium vanbaalenii |
| 5.1.1.10 | gene SM0020_01805, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109 | Sinorhizobium meliloti |
| 5.1.1.10 | gene SMc02413, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109 | Sinorhizobium meliloti |
| 5.1.1.15 | gene ABI14443, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109 | Brucella anthropi |
| 5.1.1.15 | gene ACLR or Oant_4493, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109 | Brucella anthropi |
| 5.1.1.15 | gene ACLR or Smed_5339, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109 | Sinorhizobium medicae |
| 5.1.1.15 | gene ACLR, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109 | Achromobacter obae |
| 5.1.1.15 | gene CSE45_2055, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109 | Glutamicibacter nicotianae |
| 5.1.1.15 | gene CSE45_2055, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109 | Citreicella sp. SE45 |
| 5.1.1.15 | gene JNB_04915, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109 | Janibacter sp. HTCC2649 |
| 5.1.1.15 | gene Mesop_2670, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109 | Mesorhizobium opportunistum |
| 5.1.1.15 | gene Mvan_2918, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109 | Mycolicibacterium vanbaalenii |
| 5.1.1.15 | gene SM0020_01805, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109 | Sinorhizobium meliloti |
| 5.1.1.15 | gene SMc02413, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109 | Sinorhizobium meliloti |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.1.1.10 | L-2-aminohexano-6-lactam | Achromobacter obae | - |
D-2-aminohexano-6-lactam | - |
r |  |
| 5.1.1.10 | additional information | Brucella anthropi | 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 | ? | - |
? | |
| 5.1.1.10 | additional information | Glutamicibacter nicotianae | the enzyme encoded by gene CQ758817 shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams | ? | - |
? | |
| 5.1.1.10 | additional information | Citreicella sp. SE45 | 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 | ? | - |
? | |
| 5.1.1.10 | additional information | Janibacter sp. HTCC2649 | 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 | ? | - |
? | |
| 5.1.1.10 | additional information | Mesorhizobium opportunistum | 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 | ? | - |
? | |
| 5.1.1.10 | additional information | Mycolicibacterium vanbaalenii | 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 | ? | - |
? | |
| 5.1.1.10 | additional information | Brucella anthropi | 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 | ? | - |
? | |
| 5.1.1.10 | additional information | Sinorhizobium meliloti | 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 | ? | - |
? | |
| 5.1.1.10 | additional information | Sinorhizobium meliloti | 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 | ? | - |
? | |
| 5.1.1.10 | additional information | Sinorhizobium medicae | 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 | ? | - |
? | |
| 5.1.1.10 | additional information | Mesorhizobium opportunistum WSM 2075 | 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 | ? | - |
? | |
| 5.1.1.10 | additional information | Sinorhizobium meliloti CCNWSX0020 | 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 | ? | - |
? | |
| 5.1.1.10 | additional information | Sinorhizobium medicae WSM 419 | 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 | ? | - |
? | |
| 5.1.1.10 | additional information | Mycolicibacterium vanbaalenii PYR-1 | 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 | ? | - |
? | |
| 5.1.1.10 | additional information | Glutamicibacter nicotianae NCIMB 41126 | the enzyme encoded by gene CQ758817 shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams | ? | - |
? | |
| 5.1.1.10 | additional information | Brucella anthropi IA / NCBIMB41129 | 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 | ? | - |
? | |
| 5.1.1.10 | additional information | Brucella anthropi ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168 | 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 | ? | - |
? | |
| 5.1.1.15 | L-2-aminohexano-6-lactam | Achromobacter obae | - |
D-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.15 | additional information | Brucella anthropi | 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 | ? | - |
? | |
| 5.1.1.15 | additional information | Glutamicibacter nicotianae | the enzyme encoded by gene CQ758817 shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams | ? | - |
? | |
| 5.1.1.15 | additional information | Citreicella sp. SE45 | 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 | ? | - |
? | |
| 5.1.1.15 | additional information | Janibacter sp. HTCC2649 | 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 | ? | - |
? | |
| 5.1.1.15 | additional information | Mesorhizobium opportunistum | 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 | ? | - |
? | |
| 5.1.1.15 | additional information | Mycolicibacterium vanbaalenii | 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 | ? | - |
? | |
| 5.1.1.15 | additional information | Brucella anthropi | 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 | ? | - |
? | |
| 5.1.1.15 | additional information | Sinorhizobium meliloti | 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 | ? | - |
? | |
| 5.1.1.15 | additional information | Sinorhizobium meliloti | 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 | ? | - |
? | |
| 5.1.1.15 | additional information | Sinorhizobium medicae | 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 | ? | - |
? | |
| 5.1.1.15 | additional information | Brucella anthropi IA / NCBIMB41129 | 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 | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.1.1.10 | Achromobacter obae | Q7M181 | - |
- |
| 5.1.1.10 | Brucella anthropi | A6X7I5 | - |
- |
| 5.1.1.10 | Brucella anthropi | Q06K28 | - |
- |
| 5.1.1.10 | Brucella anthropi ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168 | A6X7I5 | - |
- |
| 5.1.1.10 | Brucella anthropi IA / NCBIMB41129 | Q06K28 | - |
- |
| 5.1.1.10 | Citreicella sp. SE45 | - |
- |
- |
| 5.1.1.10 | Glutamicibacter nicotianae | - |
- |
- |
| 5.1.1.10 | Glutamicibacter nicotianae NCIMB 41126 | - |
- |
- |
| 5.1.1.10 | Janibacter sp. HTCC2649 | A3TM80 | - |
- |
| 5.1.1.10 | Mesorhizobium opportunistum | F7Y223 | - |
- |
| 5.1.1.10 | Mesorhizobium opportunistum WSM 2075 | F7Y223 | - |
- |
| 5.1.1.10 | Mycolicibacterium vanbaalenii | A1T974 | - |
- |
| 5.1.1.10 | Mycolicibacterium vanbaalenii PYR-1 | A1T974 | - |
- |
| 5.1.1.10 | Sinorhizobium medicae | A6UKD1 | i.e. Ensifer medicae strain WSM 419 | - |
| 5.1.1.10 | Sinorhizobium medicae WSM 419 | A6UKD1 | i.e. Ensifer medicae strain WSM 419 | - |
| 5.1.1.10 | Sinorhizobium meliloti | H0FT96 | - |
- |
| 5.1.1.10 | Sinorhizobium meliloti | Q92MM4 | - |
- |
| 5.1.1.10 | Sinorhizobium meliloti CCNWSX0020 | H0FT96 | - |
- |
| 5.1.1.15 | Achromobacter obae | Q7M181 | - |
- |
| 5.1.1.15 | Brucella anthropi | - |
- |
- |
| 5.1.1.15 | Brucella anthropi | A6X7I5 | - |
- |
| 5.1.1.15 | Brucella anthropi ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168 | A6X7I5 | - |
- |
| 5.1.1.15 | Brucella anthropi IA / NCBIMB41129 | - |
- |
- |
| 5.1.1.15 | Citreicella sp. SE45 | - |
- |
- |
| 5.1.1.15 | Glutamicibacter nicotianae | - |
- |
- |
| 5.1.1.15 | Glutamicibacter nicotianae NCIMB 41126 | - |
- |
- |
| 5.1.1.15 | Janibacter sp. HTCC2649 | A3TM80 | - |
- |
| 5.1.1.15 | Mesorhizobium opportunistum | F7Y223 | - |
- |
| 5.1.1.15 | Mesorhizobium opportunistum WSM 2075 | F7Y223 | - |
- |
| 5.1.1.15 | Mycolicibacterium vanbaalenii | A1T974 | - |
- |
| 5.1.1.15 | Mycolicibacterium vanbaalenii PYR-1 | A1T974 | - |
- |
| 5.1.1.15 | Sinorhizobium medicae | A6UKD1 | i.e. Ensifer medicae strain WSM 419 | - |
| 5.1.1.15 | Sinorhizobium medicae WSM 419 | A6UKD1 | i.e. Ensifer medicae strain WSM 419 | - |
| 5.1.1.15 | Sinorhizobium meliloti | H0FT96 | - |
- |
| 5.1.1.15 | Sinorhizobium meliloti | Q92MM4 | - |
- |
| 5.1.1.15 | Sinorhizobium meliloti CCNWSX0020 | H0FT96 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 5.1.1.10 | recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis | Glutamicibacter nicotianae |
| 5.1.1.10 | recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis | Achromobacter obae |
| 5.1.1.10 | recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis | Sinorhizobium medicae |
| 5.1.1.10 | recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis | Sinorhizobium meliloti |
| 5.1.1.10 | recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis | Janibacter sp. HTCC2649 |
| 5.1.1.10 | recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis | Mesorhizobium opportunistum |
| 5.1.1.10 | recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis | Mycolicibacterium vanbaalenii |
| 5.1.1.10 | recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis | Brucella anthropi |
| 5.1.1.10 | recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis | Citreicella sp. SE45 |
| 5.1.1.15 | recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis | Brucella anthropi |
| 5.1.1.15 | recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis | Glutamicibacter nicotianae |
| 5.1.1.15 | recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis | Achromobacter obae |
| 5.1.1.15 | recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis | Sinorhizobium medicae |
| 5.1.1.15 | recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis | Sinorhizobium meliloti |
| 5.1.1.15 | recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis | Janibacter sp. HTCC2649 |
| 5.1.1.15 | recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis | Mesorhizobium opportunistum |
| 5.1.1.15 | recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis | Mycolicibacterium vanbaalenii |
| 5.1.1.15 | recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis | Citreicella sp. SE45 |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 5.1.1.10 | an L-amino acid = a D-amino acid | the racemization of ACL racemase proceeds via a two-base mechanism | Achromobacter obae | |
| 5.1.1.15 | (S)-2-aminohexano-6-lactam = (R)-2-aminohexano-6-lactam | the racemization of ACL racemase proceeds via a two-base mechanism | Achromobacter obae |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 5.1.1.10 | 11 | - |
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C | Brucella anthropi |
| 5.1.1.10 | 20 | - |
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C | Mycolicibacterium vanbaalenii |
| 5.1.1.10 | 39 | - |
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C | Mesorhizobium opportunistum |
| 5.1.1.10 | 47 | - |
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C | Janibacter sp. HTCC2649 |
| 5.1.1.10 | 63 | - |
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C | Brucella anthropi |
| 5.1.1.10 | 63 | - |
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C | Janibacter sp. HTCC2649 |
| 5.1.1.10 | 68 | - |
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C | Sinorhizobium meliloti |
| 5.1.1.10 | 94 | - |
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C | Mycolicibacterium vanbaalenii |
| 5.1.1.10 | 105 | - |
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C | Sinorhizobium meliloti |
| 5.1.1.10 | 107 | - |
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C | Sinorhizobium meliloti |
| 5.1.1.10 | 133 | - |
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C | Mesorhizobium opportunistum |
| 5.1.1.10 | 182 | - |
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C | Glutamicibacter nicotianae |
| 5.1.1.10 | 260 | - |
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C | Sinorhizobium meliloti |
| 5.1.1.10 | 422 | - |
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C | Glutamicibacter nicotianae |
| 5.1.1.10 | 443 | - |
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C | Achromobacter obae |
| 5.1.1.10 | 444 | - |
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 8.0, 30°C | Brucella anthropi |
| 5.1.1.10 | 520 | - |
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C | Sinorhizobium medicae |
| 5.1.1.10 | 627 | - |
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C | Achromobacter obae |
| 5.1.1.10 | 681 | - |
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.5, 30°C | Citreicella sp. SE45 |
| 5.1.1.10 | 772 | - |
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.5, 30°C | Citreicella sp. SE45 |
| 5.1.1.10 | 1072 | - |
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C | Sinorhizobium medicae |
| 5.1.1.10 | 1225 | - |
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 8.0, 30°C | Brucella anthropi |
| 5.1.1.15 | 11 | - |
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C | Brucella anthropi |
| 5.1.1.15 | 20 | - |
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C | Mycolicibacterium vanbaalenii |
| 5.1.1.15 | 39 | - |
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C | Mesorhizobium opportunistum |
| 5.1.1.15 | 47 | - |
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C | Janibacter sp. HTCC2649 |
| 5.1.1.15 | 63 | - |
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C | Brucella anthropi |
| 5.1.1.15 | 63 | - |
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C | Janibacter sp. HTCC2649 |
| 5.1.1.15 | 68 | - |
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C | Sinorhizobium meliloti |
| 5.1.1.15 | 94 | - |
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C | Mycolicibacterium vanbaalenii |
| 5.1.1.15 | 105 | - |
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C | Sinorhizobium meliloti |
| 5.1.1.15 | 107 | - |
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C | Sinorhizobium meliloti |
| 5.1.1.15 | 133 | - |
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C | Mesorhizobium opportunistum |
| 5.1.1.15 | 182 | - |
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C | Glutamicibacter nicotianae |
| 5.1.1.15 | 260 | - |
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C | Sinorhizobium meliloti |
| 5.1.1.15 | 422 | - |
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C | Glutamicibacter nicotianae |
| 5.1.1.15 | 443 | - |
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C | Achromobacter obae |
| 5.1.1.15 | 444 | - |
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 8.0, 30°C | Brucella anthropi |
| 5.1.1.15 | 520 | - |
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C | Sinorhizobium medicae |
| 5.1.1.15 | 627 | - |
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C | Achromobacter obae |
| 5.1.1.15 | 681 | - |
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.5, 30°C | Citreicella sp. SE45 |
| 5.1.1.15 | 772 | - |
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.5, 30°C | Citreicella sp. SE45 |
| 5.1.1.15 | 1072 | - |
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C | Sinorhizobium medicae |
| 5.1.1.15 | 1225 | - |
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 8.0, 30°C | Brucella anthropi |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.1.1.10 | D-2-aminohexano-6-lactam | - |
Glutamicibacter nicotianae | L-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.10 | D-2-aminohexano-6-lactam | - |
Achromobacter obae | L-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.10 | D-2-aminohexano-6-lactam | - |
Sinorhizobium medicae | L-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.10 | D-2-aminohexano-6-lactam | - |
Sinorhizobium meliloti | L-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.10 | D-2-aminohexano-6-lactam | - |
Janibacter sp. HTCC2649 | L-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.10 | D-2-aminohexano-6-lactam | - |
Mesorhizobium opportunistum | L-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.10 | D-2-aminohexano-6-lactam | - |
Mycolicibacterium vanbaalenii | L-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.10 | D-2-aminohexano-6-lactam | - |
Brucella anthropi | L-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.10 | D-2-aminohexano-6-lactam | - |
Citreicella sp. SE45 | L-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.10 | D-2-aminohexano-6-lactam | - |
Mesorhizobium opportunistum WSM 2075 | L-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.10 | D-2-aminohexano-6-lactam | - |
Sinorhizobium meliloti CCNWSX0020 | L-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.10 | D-2-aminohexano-6-lactam | - |
Sinorhizobium medicae WSM 419 | L-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.10 | D-2-aminohexano-6-lactam | - |
Mycolicibacterium vanbaalenii PYR-1 | L-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.10 | D-2-aminohexano-6-lactam | - |
Glutamicibacter nicotianae NCIMB 41126 | L-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.10 | D-2-aminohexano-6-lactam | - |
Brucella anthropi IA / NCBIMB41129 | L-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.10 | D-2-aminohexano-6-lactam | - |
Brucella anthropi ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168 | L-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.10 | L-2-aminohexano-6-lactam | - |
Glutamicibacter nicotianae | D-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.10 | L-2-aminohexano-6-lactam | - |
Achromobacter obae | D-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.10 | L-2-aminohexano-6-lactam | - |
Sinorhizobium medicae | D-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.10 | L-2-aminohexano-6-lactam | - |
Sinorhizobium meliloti | D-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.10 | L-2-aminohexano-6-lactam | - |
Janibacter sp. HTCC2649 | D-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.10 | L-2-aminohexano-6-lactam | - |
Mesorhizobium opportunistum | D-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.10 | L-2-aminohexano-6-lactam | - |
Mycolicibacterium vanbaalenii | D-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.10 | L-2-aminohexano-6-lactam | - |
Brucella anthropi | D-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.10 | L-2-aminohexano-6-lactam | - |
Citreicella sp. SE45 | D-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.10 | L-alanine | - |
Glutamicibacter nicotianae | D-alanine | - |
r | |
| 5.1.1.10 | L-alanine | - |
Achromobacter obae | D-alanine | - |
r | |
| 5.1.1.10 | L-alanine | - |
Sinorhizobium medicae | D-alanine | - |
r | |
| 5.1.1.10 | L-alanine | - |
Sinorhizobium meliloti | D-alanine | - |
r | |
| 5.1.1.10 | L-alanine | - |
Janibacter sp. HTCC2649 | D-alanine | - |
r | |
| 5.1.1.10 | L-alanine | - |
Mesorhizobium opportunistum | D-alanine | - |
r | |
| 5.1.1.10 | L-alanine | - |
Mycolicibacterium vanbaalenii | D-alanine | - |
r | |
| 5.1.1.10 | L-alanine | - |
Brucella anthropi | D-alanine | - |
r | |
| 5.1.1.10 | L-alanine | - |
Citreicella sp. SE45 | D-alanine | - |
r | |
| 5.1.1.10 | L-alanine | - |
Mesorhizobium opportunistum WSM 2075 | D-alanine | - |
r | |
| 5.1.1.10 | L-alanine | - |
Sinorhizobium meliloti CCNWSX0020 | D-alanine | - |
r | |
| 5.1.1.10 | L-alanine | - |
Sinorhizobium medicae WSM 419 | D-alanine | - |
r | |
| 5.1.1.10 | L-alanine | - |
Mycolicibacterium vanbaalenii PYR-1 | D-alanine | - |
r | |
| 5.1.1.10 | L-alanine | - |
Glutamicibacter nicotianae NCIMB 41126 | D-alanine | - |
r | |
| 5.1.1.10 | L-alanine | - |
Brucella anthropi IA / NCBIMB41129 | D-alanine | - |
r | |
| 5.1.1.10 | L-alanine | - |
Brucella anthropi ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168 | D-alanine | - |
r | |
| 5.1.1.10 | L-alanine amide | - |
Glutamicibacter nicotianae | D-alanine amide | - |
r | |
| 5.1.1.10 | L-alanine amide | - |
Achromobacter obae | D-alanine amide | - |
r | |
| 5.1.1.10 | L-alanine amide | - |
Sinorhizobium medicae | D-alanine amide | - |
r | |
| 5.1.1.10 | L-alanine amide | - |
Sinorhizobium meliloti | D-alanine amide | - |
r | |
| 5.1.1.10 | L-alanine amide | - |
Janibacter sp. HTCC2649 | D-alanine amide | - |
r | |
| 5.1.1.10 | L-alanine amide | - |
Mesorhizobium opportunistum | D-alanine amide | - |
r | |
| 5.1.1.10 | L-alanine amide | - |
Mycolicibacterium vanbaalenii | D-alanine amide | - |
r | |
| 5.1.1.10 | L-alanine amide | - |
Brucella anthropi | D-alanine amide | - |
r | |
| 5.1.1.10 | L-alanine amide | - |
Citreicella sp. SE45 | D-alanine amide | - |
r | |
| 5.1.1.10 | L-alanine amide | - |
Mesorhizobium opportunistum WSM 2075 | D-alanine amide | - |
r | |
| 5.1.1.10 | L-alanine amide | - |
Sinorhizobium meliloti CCNWSX0020 | D-alanine amide | - |
r | |
| 5.1.1.10 | L-alanine amide | - |
Sinorhizobium medicae WSM 419 | D-alanine amide | - |
r | |
| 5.1.1.10 | L-alanine amide | - |
Mycolicibacterium vanbaalenii PYR-1 | D-alanine amide | - |
r | |
| 5.1.1.10 | L-alanine amide | - |
Glutamicibacter nicotianae NCIMB 41126 | D-alanine amide | - |
r | |
| 5.1.1.10 | L-alanine amide | - |
Brucella anthropi IA / NCBIMB41129 | D-alanine amide | - |
r | |
| 5.1.1.10 | L-alanine amide | - |
Brucella anthropi ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168 | D-alanine amide | - |
r | |
| 5.1.1.10 | L-leucine amide | - |
Glutamicibacter nicotianae | D-leucine amide | - |
r | |
| 5.1.1.10 | L-leucine amide | - |
Achromobacter obae | D-leucine amide | - |
r | |
| 5.1.1.10 | L-leucine amide | - |
Mesorhizobium opportunistum | D-leucine amide | - |
r | |
| 5.1.1.10 | L-leucine amide | - |
Sinorhizobium meliloti | D-leucine amide | - |
r | |
| 5.1.1.10 | L-leucine amide | - |
Citreicella sp. SE45 | D-leucine amide | - |
r | |
| 5.1.1.10 | L-methionine amide | - |
Glutamicibacter nicotianae | D-methionine amide | - |
r | |
| 5.1.1.10 | L-methionine amide | - |
Achromobacter obae | D-methionine amide | - |
r | |
| 5.1.1.10 | L-methionine amide | - |
Sinorhizobium medicae | D-methionine amide | - |
r | |
| 5.1.1.10 | L-methionine amide | - |
Sinorhizobium meliloti | D-methionine amide | - |
r | |
| 5.1.1.10 | L-methionine amide | - |
Janibacter sp. HTCC2649 | D-methionine amide | - |
r | |
| 5.1.1.10 | L-methionine amide | - |
Mesorhizobium opportunistum | D-methionine amide | - |
r | |
| 5.1.1.10 | L-methionine amide | - |
Mycolicibacterium vanbaalenii | D-methionine amide | - |
r | |
| 5.1.1.10 | L-methionine amide | - |
Brucella anthropi | D-methionine amide | - |
r | |
| 5.1.1.10 | L-methionine amide | - |
Citreicella sp. SE45 | D-methionine amide | - |
r | |
| 5.1.1.10 | L-phenylalanine amide | - |
Glutamicibacter nicotianae | D-phenylalanine amide | - |
r | |
| 5.1.1.10 | L-phenylalanine amide | - |
Achromobacter obae | D-phenylalanine amide | - |
r | |
| 5.1.1.10 | L-phenylalanine amide | - |
Sinorhizobium medicae | D-phenylalanine amide | - |
r | |
| 5.1.1.10 | L-phenylalanine amide | - |
Sinorhizobium meliloti | D-phenylalanine amide | - |
r | |
| 5.1.1.10 | L-phenylalanine amide | - |
Janibacter sp. HTCC2649 | D-phenylalanine amide | - |
r | |
| 5.1.1.10 | L-phenylalanine amide | - |
Mesorhizobium opportunistum | D-phenylalanine amide | - |
r | |
| 5.1.1.10 | L-phenylalanine amide | - |
Mycolicibacterium vanbaalenii | D-phenylalanine amide | - |
r | |
| 5.1.1.10 | L-phenylalanine amide | - |
Brucella anthropi | D-phenylalanine amide | - |
r | |
| 5.1.1.10 | L-phenylalanine amide | - |
Citreicella sp. SE45 | D-phenylalanine amide | - |
r | |
| 5.1.1.10 | L-phenylglycine amide | - |
Glutamicibacter nicotianae | D-phenylglycine amide | - |
r | |
| 5.1.1.10 | L-phenylglycine amide | - |
Achromobacter obae | D-phenylglycine amide | - |
r | |
| 5.1.1.10 | L-phenylglycine amide | - |
Sinorhizobium medicae | D-phenylglycine amide | - |
r | |
| 5.1.1.10 | L-phenylglycine amide | - |
Sinorhizobium meliloti | D-phenylglycine amide | - |
r | |
| 5.1.1.10 | L-phenylglycine amide | - |
Janibacter sp. HTCC2649 | D-phenylglycine amide | - |
r | |
| 5.1.1.10 | L-phenylglycine amide | - |
Mesorhizobium opportunistum | D-phenylglycine amide | - |
r | |
| 5.1.1.10 | L-phenylglycine amide | - |
Mycolicibacterium vanbaalenii | D-phenylglycine amide | - |
r | |
| 5.1.1.10 | L-phenylglycine amide | - |
Brucella anthropi | D-phenylglycine amide | - |
r | |
| 5.1.1.10 | L-phenylglycine amide | - |
Citreicella sp. SE45 | D-phenylglycine amide | - |
r | |
| 5.1.1.10 | L-serine amide | - |
Glutamicibacter nicotianae | D-serine amide | - |
r | |
| 5.1.1.10 | L-serine amide | - |
Achromobacter obae | D-serine amide | - |
r | |
| 5.1.1.10 | L-serine amide | - |
Sinorhizobium medicae | D-serine amide | - |
r | |
| 5.1.1.10 | L-serine amide | - |
Sinorhizobium meliloti | D-serine amide | - |
r | |
| 5.1.1.10 | L-serine amide | - |
Janibacter sp. HTCC2649 | D-serine amide | - |
r | |
| 5.1.1.10 | L-serine amide | - |
Mesorhizobium opportunistum | D-serine amide | - |
r | |
| 5.1.1.10 | L-serine amide | - |
Brucella anthropi | D-serine amide | - |
r | |
| 5.1.1.10 | L-serine amide | - |
Citreicella sp. SE45 | D-serine amide | - |
r | |
| 5.1.1.10 | L-tyrosine amide | - |
Glutamicibacter nicotianae | D-tyrosine amide | - |
r | |
| 5.1.1.10 | L-tyrosine amide | - |
Sinorhizobium medicae | D-tyrosine amide | - |
r | |
| 5.1.1.10 | L-tyrosine amide | - |
Mesorhizobium opportunistum | D-tyrosine amide | - |
r | |
| 5.1.1.10 | L-tyrosine amide | - |
Sinorhizobium meliloti | D-tyrosine amide | - |
r | |
| 5.1.1.10 | L-tyrosine amide | - |
Brucella anthropi | D-tyrosine amide | - |
r | |
| 5.1.1.10 | L-valine amide | - |
Glutamicibacter nicotianae | D-valine amide | - |
r | |
| 5.1.1.10 | L-valine amide | - |
Achromobacter obae | D-valine amide | - |
r | |
| 5.1.1.10 | L-valine amide | - |
Sinorhizobium medicae | D-valine amide | - |
r | |
| 5.1.1.10 | L-valine amide | - |
Sinorhizobium meliloti | D-valine amide | - |
r | |
| 5.1.1.10 | L-valine amide | - |
Janibacter sp. HTCC2649 | D-valine amide | - |
r | |
| 5.1.1.10 | L-valine amide | - |
Mesorhizobium opportunistum | D-valine amide | - |
r | |
| 5.1.1.10 | L-valine amide | - |
Mycolicibacterium vanbaalenii | D-valine amide | - |
r | |
| 5.1.1.10 | L-valine amide | - |
Brucella anthropi | D-valine amide | - |
r | |
| 5.1.1.10 | L-valine amide | - |
Citreicella sp. SE45 | D-valine amide | - |
r | |
| 5.1.1.10 | 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 | ? | - |
? | |
| 5.1.1.10 | 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 | ? | - |
? | |
| 5.1.1.10 | 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 | ? | - |
? | |
| 5.1.1.10 | 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 | ? | - |
? | |
| 5.1.1.10 | 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 | ? | - |
? | |
| 5.1.1.10 | 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 | ? | - |
? | |
| 5.1.1.10 | 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 | ? | - |
? | |
| 5.1.1.10 | 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 | ? | - |
? | |
| 5.1.1.10 | 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 | ? | - |
? | |
| 5.1.1.10 | 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 | ? | - |
? | |
| 5.1.1.10 | additional information | the enzyme is active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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 | Citreicella sp. SE45 | ? | - |
? | |
| 5.1.1.10 | additional information | the enzyme is active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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 | Sinorhizobium meliloti | ? | - |
? | |
| 5.1.1.10 | additional information | the enzyme is active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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 | Sinorhizobium meliloti | ? | - |
? | |
| 5.1.1.10 | additional information | the enzyme is active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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 | Janibacter sp. HTCC2649 | ? | - |
? | |
| 5.1.1.10 | additional information | the enzyme is active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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 | Brucella anthropi | ? | - |
? | |
| 5.1.1.10 | additional information | the enzyme is active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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 | Achromobacter obae | ? | - |
? | |
| 5.1.1.10 | additional information | the enzyme is active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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 | Glutamicibacter nicotianae | ? | - |
? | |
| 5.1.1.10 | additional information | the enzyme is active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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 | Mesorhizobium opportunistum | ? | - |
? | |
| 5.1.1.10 | additional information | the enzyme is active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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 | Sinorhizobium medicae | ? | - |
? | |
| 5.1.1.10 | additional information | the enzyme is active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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 | Brucella anthropi | ? | - |
? | |
| 5.1.1.10 | additional information | the enzyme is active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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 | Mycolicibacterium vanbaalenii | ? | - |
? | |
| 5.1.1.10 | 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 WSM 2075 | ? | - |
? | |
| 5.1.1.10 | additional information | the enzyme is active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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 | Mesorhizobium opportunistum WSM 2075 | ? | - |
? | |
| 5.1.1.10 | 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 CCNWSX0020 | ? | - |
? | |
| 5.1.1.10 | additional information | the enzyme is active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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 | Sinorhizobium meliloti CCNWSX0020 | ? | - |
? | |
| 5.1.1.10 | 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 WSM 419 | ? | - |
? | |
| 5.1.1.10 | additional information | the enzyme is active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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 | Sinorhizobium medicae WSM 419 | ? | - |
? | |
| 5.1.1.10 | 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 PYR-1 | ? | - |
? | |
| 5.1.1.10 | additional information | the enzyme is active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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 | Mycolicibacterium vanbaalenii PYR-1 | ? | - |
? | |
| 5.1.1.10 | 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 NCIMB 41126 | ? | - |
? | |
| 5.1.1.10 | additional information | the enzyme is active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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 | Glutamicibacter nicotianae NCIMB 41126 | ? | - |
? | |
| 5.1.1.10 | 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 | ? | - |
? | |
| 5.1.1.10 | additional information | the enzyme is active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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 | Brucella anthropi IA / NCBIMB41129 | ? | - |
? | |
| 5.1.1.10 | 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 ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168 | ? | - |
? | |
| 5.1.1.10 | additional information | the enzyme is active on L-2-aminohexano-6-lactam, D-2-aminohexano-6-lactam, 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 | Brucella anthropi ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168 | ? | - |
? | |
| 5.1.1.15 | D-2-aminohexano-6-lactam | - |
Brucella anthropi | L-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.15 | D-2-aminohexano-6-lactam | - |
Glutamicibacter nicotianae | L-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.15 | D-2-aminohexano-6-lactam | - |
Achromobacter obae | L-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.15 | D-2-aminohexano-6-lactam | - |
Sinorhizobium medicae | L-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.15 | D-2-aminohexano-6-lactam | - |
Sinorhizobium meliloti | L-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.15 | D-2-aminohexano-6-lactam | - |
Janibacter sp. HTCC2649 | L-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.15 | D-2-aminohexano-6-lactam | - |
Mesorhizobium opportunistum | L-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.15 | D-2-aminohexano-6-lactam | - |
Mycolicibacterium vanbaalenii | L-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.15 | D-2-aminohexano-6-lactam | - |
Citreicella sp. SE45 | L-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.15 | D-2-aminohexano-6-lactam | - |
Brucella anthropi IA / NCBIMB41129 | L-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.15 | L-2-aminohexano-6-lactam | - |
Brucella anthropi | D-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.15 | L-2-aminohexano-6-lactam | - |
Glutamicibacter nicotianae | D-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.15 | L-2-aminohexano-6-lactam | - |
Achromobacter obae | D-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.15 | L-2-aminohexano-6-lactam | - |
Sinorhizobium medicae | D-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.15 | L-2-aminohexano-6-lactam | - |
Sinorhizobium meliloti | D-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.15 | L-2-aminohexano-6-lactam | - |
Janibacter sp. HTCC2649 | D-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.15 | L-2-aminohexano-6-lactam | - |
Mesorhizobium opportunistum | D-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.15 | L-2-aminohexano-6-lactam | - |
Mycolicibacterium vanbaalenii | D-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.15 | L-2-aminohexano-6-lactam | - |
Citreicella sp. SE45 | D-2-aminohexano-6-lactam | - |
r | |
| 5.1.1.15 | L-2-aminohexano-6-lactam | - |
Brucella anthropi IA / NCBIMB41129 | D-2-aminohexano-6-lactam | - |
r | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.1.1.10 | ACL racemase | - |
Glutamicibacter nicotianae |
| 5.1.1.10 | ACL racemase | - |
Achromobacter obae |
| 5.1.1.10 | ACL racemase | - |
Sinorhizobium medicae |
| 5.1.1.10 | ACL racemase | - |
Sinorhizobium meliloti |
| 5.1.1.10 | ACL racemase | - |
Janibacter sp. HTCC2649 |
| 5.1.1.10 | ACL racemase | - |
Mesorhizobium opportunistum |
| 5.1.1.10 | ACL racemase | - |
Mycolicibacterium vanbaalenii |
| 5.1.1.10 | ACL racemase | - |
Brucella anthropi |
| 5.1.1.10 | ACL racemase | - |
Citreicella sp. SE45 |
| 5.1.1.10 | More | cf. EC 5.1.1.15 | Glutamicibacter nicotianae |
| 5.1.1.10 | More | cf. EC 5.1.1.15 | Achromobacter obae |
| 5.1.1.10 | More | cf. EC 5.1.1.15 | Sinorhizobium medicae |
| 5.1.1.10 | More | cf. EC 5.1.1.15 | Sinorhizobium meliloti |
| 5.1.1.10 | More | cf. EC 5.1.1.15 | Janibacter sp. HTCC2649 |
| 5.1.1.10 | More | cf. EC 5.1.1.15 | Mesorhizobium opportunistum |
| 5.1.1.10 | More | cf. EC 5.1.1.15 | Mycolicibacterium vanbaalenii |
| 5.1.1.10 | More | cf. EC 5.1.1.15 | Brucella anthropi |
| 5.1.1.10 | More | cf. EC 5.1.1.15 | Citreicella sp. SE45 |
| 5.1.1.15 | ACL racemase | - |
Brucella anthropi |
| 5.1.1.15 | ACL racemase | - |
Glutamicibacter nicotianae |
| 5.1.1.15 | ACL racemase | - |
Achromobacter obae |
| 5.1.1.15 | ACL racemase | - |
Sinorhizobium medicae |
| 5.1.1.15 | ACL racemase | - |
Sinorhizobium meliloti |
| 5.1.1.15 | ACL racemase | - |
Janibacter sp. HTCC2649 |
| 5.1.1.15 | ACL racemase | - |
Mesorhizobium opportunistum |
| 5.1.1.15 | ACL racemase | - |
Mycolicibacterium vanbaalenii |
| 5.1.1.15 | ACL racemase | - |
Citreicella sp. SE45 |
| 5.1.1.15 | alpha-Amino-epsilon-caprolactam racemase | - |
Brucella anthropi |
| 5.1.1.15 | alpha-Amino-epsilon-caprolactam racemase | - |
Glutamicibacter nicotianae |
| 5.1.1.15 | alpha-Amino-epsilon-caprolactam racemase | - |
Achromobacter obae |
| 5.1.1.15 | alpha-Amino-epsilon-caprolactam racemase | - |
Sinorhizobium medicae |
| 5.1.1.15 | alpha-Amino-epsilon-caprolactam racemase | - |
Sinorhizobium meliloti |
| 5.1.1.15 | alpha-Amino-epsilon-caprolactam racemase | - |
Janibacter sp. HTCC2649 |
| 5.1.1.15 | alpha-Amino-epsilon-caprolactam racemase | - |
Mesorhizobium opportunistum |
| 5.1.1.15 | alpha-Amino-epsilon-caprolactam racemase | - |
Mycolicibacterium vanbaalenii |
| 5.1.1.15 | alpha-Amino-epsilon-caprolactam racemase | - |
Citreicella sp. SE45 |
| 5.1.1.15 | moe | cf. EC 5.1.1.10 | Sinorhizobium medicae |
| 5.1.1.15 | More | cf. EC 5.1.1.10 | Brucella anthropi |
| 5.1.1.15 | More | cf. EC 5.1.1.10 | Glutamicibacter nicotianae |
| 5.1.1.15 | More | cf. EC 5.1.1.10 | Achromobacter obae |
| 5.1.1.15 | More | cf. EC 5.1.1.10 | Sinorhizobium meliloti |
| 5.1.1.15 | More | cf. EC 5.1.1.10 | Janibacter sp. HTCC2649 |
| 5.1.1.15 | More | cf. EC 5.1.1.10 | Mesorhizobium opportunistum |
| 5.1.1.15 | More | cf. EC 5.1.1.10 | Mycolicibacterium vanbaalenii |
| 5.1.1.15 | More | cf. EC 5.1.1.10 | Citreicella sp. SE45 |
| 5.1.1.15 | SMc02413 | - |
Sinorhizobium meliloti |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.1.1.10 | 30 | - |
assay at | Glutamicibacter nicotianae |
| 5.1.1.10 | 30 | - |
assay at | Achromobacter obae |
| 5.1.1.10 | 30 | - |
assay at | Sinorhizobium medicae |
| 5.1.1.10 | 30 | - |
assay at | Sinorhizobium meliloti |
| 5.1.1.10 | 30 | - |
assay at | Janibacter sp. HTCC2649 |
| 5.1.1.10 | 30 | - |
assay at | Mesorhizobium opportunistum |
| 5.1.1.10 | 30 | - |
assay at | Mycolicibacterium vanbaalenii |
| 5.1.1.10 | 30 | - |
assay at | Brucella anthropi |
| 5.1.1.10 | 30 | - |
assay at | Citreicella sp. SE45 |
| 5.1.1.15 | 30 | - |
assay at | Brucella anthropi |
| 5.1.1.15 | 30 | - |
assay at | Glutamicibacter nicotianae |
| 5.1.1.15 | 30 | - |
assay at | Achromobacter obae |
| 5.1.1.15 | 30 | - |
assay at | Sinorhizobium medicae |
| 5.1.1.15 | 30 | - |
assay at | Sinorhizobium meliloti |
| 5.1.1.15 | 30 | - |
assay at | Janibacter sp. HTCC2649 |
| 5.1.1.15 | 30 | - |
assay at | Mesorhizobium opportunistum |
| 5.1.1.15 | 30 | - |
assay at | Mycolicibacterium vanbaalenii |
| 5.1.1.15 | 30 | - |
assay at | Citreicella sp. SE45 |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.1.1.10 | 7 | - |
assay at | Glutamicibacter nicotianae |
| 5.1.1.10 | 7 | - |
assay at | Achromobacter obae |
| 5.1.1.10 | 7 | - |
assay at | Sinorhizobium medicae |
| 5.1.1.10 | 7 | - |
assay at | Sinorhizobium meliloti |
| 5.1.1.10 | 7 | - |
assay at | Janibacter sp. HTCC2649 |
| 5.1.1.10 | 7 | - |
assay at | Mesorhizobium opportunistum |
| 5.1.1.10 | 7 | - |
assay at | Mycolicibacterium vanbaalenii |
| 5.1.1.10 | 7 | - |
assay at | Brucella anthropi |
| 5.1.1.10 | 7.5 | - |
assay at | Citreicella sp. SE45 |
| 5.1.1.10 | 8 | - |
assay at | Brucella anthropi |
| 5.1.1.15 | 7 | - |
assay at | Brucella anthropi |
| 5.1.1.15 | 7 | - |
assay at | Glutamicibacter nicotianae |
| 5.1.1.15 | 7 | - |
assay at | Achromobacter obae |
| 5.1.1.15 | 7 | - |
assay at | Sinorhizobium medicae |
| 5.1.1.15 | 7 | - |
assay at | Sinorhizobium meliloti |
| 5.1.1.15 | 7 | - |
assay at | Janibacter sp. HTCC2649 |
| 5.1.1.15 | 7 | - |
assay at | Mesorhizobium opportunistum |
| 5.1.1.15 | 7 | - |
assay at | Mycolicibacterium vanbaalenii |
| 5.1.1.15 | 7.5 | - |
assay at | Citreicella sp. SE45 |
| 5.1.1.15 | 8 | - |
assay at | Brucella anthropi |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.1.1.10 | pyridoxal 5'-phosphate | PLP, the enzyme is a fold-type I PLP-dependent enzyme | Achromobacter obae | |
| 5.1.1.15 | pyridoxal 5'-phosphate | PLP, the enzyme is a fold-type I PLP-dependent enzyme | Achromobacter obae | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 5.1.1.10 | evolution | the enzyme belongs to the fold-type I PLP-dependent enzyme family | Achromobacter obae |
| 5.1.1.10 | malfunction | the mutation of either Asp210 or Lys267 to alanine abolish the racemization activity for 2-aminohexano-6-lactam | Achromobacter obae |
| 5.1.1.10 | additional information | analysis of the structure-function relationship, overview. Lys241 is a key amino acid residue, active site structure of ACL racemase. The substrate binding site is typically located between Trp49 and Tyr137. Lys241 Nepsilon is considered to be important for recognizing the carbonyl O of the substrate. Lys241 also forms a salt bridge with Glu396. Asp210 and Lys267 are two plausible acid/base catalytic candidate residues, situated on the re and si faces of the pyridoxal 5'-phosphate ring, respectively. The racemization of ACL racemase proceeds via a two-base mechanism | Achromobacter obae |
| 5.1.1.15 | evolution | the enzyme belongs to the fold-type I PLP-dependent enzyme family | Achromobacter obae |
| 5.1.1.15 | malfunction | the mutation of either Asp210 or Lys267 to alanine abolish the racemization activity for 2-aminohexano-6-lactam | Achromobacter obae |
| 5.1.1.15 | additional information | analysis of the structure-function relationship, overview. Lys241 is a key amino acid residue, active site structure of ACL racemase. The substrate binding site is typically located between Trp49 and Tyr137. Lys241 Nepsilon is considered to be important for recognizing the carbonyl O of the substrate. Lys241 also forms a salt bridge with Glu396. Asp210 and Lys267 are two plausible acid/base catalytic candidate residues, situated on the re and si faces of the pyridoxal 5'-phosphate ring, respectively. The racemization of ACL racemase proceeds via a two-base mechanism | Achromobacter obae |
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Release 2023.1 (January 2023)
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