Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.1.1.10 extracted from

  • Payoungkiattikun, W.; Okazaki, S.; Nakano, S.; Ina, A.; H-Kittikun, A.; Asano, Y.
    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 .
    View publication on PubMed

Application

Application Comment Organism
synthesis the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production Glutamicibacter nicotianae
synthesis the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production Achromobacter obae
synthesis the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production Sinorhizobium medicae
synthesis the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production Sinorhizobium meliloti
synthesis the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production Janibacter sp. HTCC2649
synthesis the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production Mesorhizobium opportunistum
synthesis the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production Mycolicibacterium vanbaalenii
synthesis the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production Brucella anthropi
synthesis the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production Citreicella sp. SE45

Cloned(Commentary)

Cloned (Comment) Organism
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
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
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
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
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
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
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
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
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
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
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-2-aminohexano-6-lactam Achromobacter obae
-
D-2-aminohexano-6-lactam
-
r
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?

Organism

Organism UniProt Comment Textmining
Achromobacter obae Q7M181
-
-
Brucella anthropi A6X7I5
-
-
Brucella anthropi Q06K28
-
-
Brucella anthropi ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168 A6X7I5
-
-
Brucella anthropi IA / NCBIMB41129 Q06K28
-
-
Citreicella sp. SE45
-
-
-
Glutamicibacter nicotianae
-
-
-
Glutamicibacter nicotianae NCIMB 41126
-
-
-
Janibacter sp. HTCC2649 A3TM80
-
-
Mesorhizobium opportunistum F7Y223
-
-
Mesorhizobium opportunistum WSM 2075 F7Y223
-
-
Mycolicibacterium vanbaalenii A1T974
-
-
Mycolicibacterium vanbaalenii PYR-1 A1T974
-
-
Sinorhizobium medicae A6UKD1 i.e. Ensifer medicae strain WSM 419
-
Sinorhizobium medicae WSM 419 A6UKD1 i.e. Ensifer medicae strain WSM 419
-
Sinorhizobium meliloti H0FT96
-
-
Sinorhizobium meliloti Q92MM4
-
-
Sinorhizobium meliloti CCNWSX0020 H0FT96
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis Glutamicibacter nicotianae
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis Achromobacter obae
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis Sinorhizobium medicae
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis Sinorhizobium meliloti
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis Janibacter sp. HTCC2649
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis Mesorhizobium opportunistum
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis Mycolicibacterium vanbaalenii
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis Brucella anthropi
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis Citreicella sp. SE45

Reaction

Reaction Comment Organism Reaction ID
an L-amino acid = a D-amino acid the racemization of ACL racemase proceeds via a two-base mechanism Achromobacter obae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
11
-
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C Brucella anthropi
20
-
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C Mycolicibacterium vanbaalenii
39
-
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C Mesorhizobium opportunistum
47
-
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C Janibacter sp. HTCC2649
63
-
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C Brucella anthropi
63
-
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C Janibacter sp. HTCC2649
68
-
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C Sinorhizobium meliloti
94
-
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C Mycolicibacterium vanbaalenii
105
-
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C Sinorhizobium meliloti
107
-
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C Sinorhizobium meliloti
133
-
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C Mesorhizobium opportunistum
182
-
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C Glutamicibacter nicotianae
260
-
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C Sinorhizobium meliloti
422
-
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C Glutamicibacter nicotianae
443
-
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C Achromobacter obae
444
-
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 8.0, 30°C Brucella anthropi
520
-
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C Sinorhizobium medicae
627
-
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C Achromobacter obae
681
-
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.5, 30°C Citreicella sp. SE45
772
-
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.5, 30°C Citreicella sp. SE45
1072
-
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C Sinorhizobium medicae
1225
-
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 8.0, 30°C Brucella anthropi

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-2-aminohexano-6-lactam
-
Glutamicibacter nicotianae L-2-aminohexano-6-lactam
-
r
D-2-aminohexano-6-lactam
-
Achromobacter obae L-2-aminohexano-6-lactam
-
r
D-2-aminohexano-6-lactam
-
Sinorhizobium medicae L-2-aminohexano-6-lactam
-
r
D-2-aminohexano-6-lactam
-
Sinorhizobium meliloti L-2-aminohexano-6-lactam
-
r
D-2-aminohexano-6-lactam
-
Janibacter sp. HTCC2649 L-2-aminohexano-6-lactam
-
r
D-2-aminohexano-6-lactam
-
Mesorhizobium opportunistum L-2-aminohexano-6-lactam
-
r
D-2-aminohexano-6-lactam
-
Mycolicibacterium vanbaalenii L-2-aminohexano-6-lactam
-
r
D-2-aminohexano-6-lactam
-
Brucella anthropi L-2-aminohexano-6-lactam
-
r
D-2-aminohexano-6-lactam
-
Citreicella sp. SE45 L-2-aminohexano-6-lactam
-
r
D-2-aminohexano-6-lactam
-
Mesorhizobium opportunistum WSM 2075 L-2-aminohexano-6-lactam
-
r
D-2-aminohexano-6-lactam
-
Sinorhizobium meliloti CCNWSX0020 L-2-aminohexano-6-lactam
-
r
D-2-aminohexano-6-lactam
-
Sinorhizobium medicae WSM 419 L-2-aminohexano-6-lactam
-
r
D-2-aminohexano-6-lactam
-
Mycolicibacterium vanbaalenii PYR-1 L-2-aminohexano-6-lactam
-
r
D-2-aminohexano-6-lactam
-
Glutamicibacter nicotianae NCIMB 41126 L-2-aminohexano-6-lactam
-
r
D-2-aminohexano-6-lactam
-
Brucella anthropi IA / NCBIMB41129 L-2-aminohexano-6-lactam
-
r
D-2-aminohexano-6-lactam
-
Brucella anthropi ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168 L-2-aminohexano-6-lactam
-
r
L-2-aminohexano-6-lactam
-
Glutamicibacter nicotianae D-2-aminohexano-6-lactam
-
r
L-2-aminohexano-6-lactam
-
Achromobacter obae D-2-aminohexano-6-lactam
-
r
L-2-aminohexano-6-lactam
-
Sinorhizobium medicae D-2-aminohexano-6-lactam
-
r
L-2-aminohexano-6-lactam
-
Sinorhizobium meliloti D-2-aminohexano-6-lactam
-
r
L-2-aminohexano-6-lactam
-
Janibacter sp. HTCC2649 D-2-aminohexano-6-lactam
-
r
L-2-aminohexano-6-lactam
-
Mesorhizobium opportunistum D-2-aminohexano-6-lactam
-
r
L-2-aminohexano-6-lactam
-
Mycolicibacterium vanbaalenii D-2-aminohexano-6-lactam
-
r
L-2-aminohexano-6-lactam
-
Brucella anthropi D-2-aminohexano-6-lactam
-
r
L-2-aminohexano-6-lactam
-
Citreicella sp. SE45 D-2-aminohexano-6-lactam
-
r
L-alanine
-
Glutamicibacter nicotianae D-alanine
-
r
L-alanine
-
Achromobacter obae D-alanine
-
r
L-alanine
-
Sinorhizobium medicae D-alanine
-
r
L-alanine
-
Sinorhizobium meliloti D-alanine
-
r
L-alanine
-
Janibacter sp. HTCC2649 D-alanine
-
r
L-alanine
-
Mesorhizobium opportunistum D-alanine
-
r
L-alanine
-
Mycolicibacterium vanbaalenii D-alanine
-
r
L-alanine
-
Brucella anthropi D-alanine
-
r
L-alanine
-
Citreicella sp. SE45 D-alanine
-
r
L-alanine
-
Mesorhizobium opportunistum WSM 2075 D-alanine
-
r
L-alanine
-
Sinorhizobium meliloti CCNWSX0020 D-alanine
-
r
L-alanine
-
Sinorhizobium medicae WSM 419 D-alanine
-
r
L-alanine
-
Mycolicibacterium vanbaalenii PYR-1 D-alanine
-
r
L-alanine
-
Glutamicibacter nicotianae NCIMB 41126 D-alanine
-
r
L-alanine
-
Brucella anthropi IA / NCBIMB41129 D-alanine
-
r
L-alanine
-
Brucella anthropi ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168 D-alanine
-
r
L-alanine amide
-
Glutamicibacter nicotianae D-alanine amide
-
r
L-alanine amide
-
Achromobacter obae D-alanine amide
-
r
L-alanine amide
-
Sinorhizobium medicae D-alanine amide
-
r
L-alanine amide
-
Sinorhizobium meliloti D-alanine amide
-
r
L-alanine amide
-
Janibacter sp. HTCC2649 D-alanine amide
-
r
L-alanine amide
-
Mesorhizobium opportunistum D-alanine amide
-
r
L-alanine amide
-
Mycolicibacterium vanbaalenii D-alanine amide
-
r
L-alanine amide
-
Brucella anthropi D-alanine amide
-
r
L-alanine amide
-
Citreicella sp. SE45 D-alanine amide
-
r
L-alanine amide
-
Mesorhizobium opportunistum WSM 2075 D-alanine amide
-
r
L-alanine amide
-
Sinorhizobium meliloti CCNWSX0020 D-alanine amide
-
r
L-alanine amide
-
Sinorhizobium medicae WSM 419 D-alanine amide
-
r
L-alanine amide
-
Mycolicibacterium vanbaalenii PYR-1 D-alanine amide
-
r
L-alanine amide
-
Glutamicibacter nicotianae NCIMB 41126 D-alanine amide
-
r
L-alanine amide
-
Brucella anthropi IA / NCBIMB41129 D-alanine amide
-
r
L-alanine amide
-
Brucella anthropi ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168 D-alanine amide
-
r
L-leucine amide
-
Glutamicibacter nicotianae D-leucine amide
-
r
L-leucine amide
-
Achromobacter obae D-leucine amide
-
r
L-leucine amide
-
Mesorhizobium opportunistum D-leucine amide
-
r
L-leucine amide
-
Sinorhizobium meliloti D-leucine amide
-
r
L-leucine amide
-
Citreicella sp. SE45 D-leucine amide
-
r
L-methionine amide
-
Glutamicibacter nicotianae D-methionine amide
-
r
L-methionine amide
-
Achromobacter obae D-methionine amide
-
r
L-methionine amide
-
Sinorhizobium medicae D-methionine amide
-
r
L-methionine amide
-
Sinorhizobium meliloti D-methionine amide
-
r
L-methionine amide
-
Janibacter sp. HTCC2649 D-methionine amide
-
r
L-methionine amide
-
Mesorhizobium opportunistum D-methionine amide
-
r
L-methionine amide
-
Mycolicibacterium vanbaalenii D-methionine amide
-
r
L-methionine amide
-
Brucella anthropi D-methionine amide
-
r
L-methionine amide
-
Citreicella sp. SE45 D-methionine amide
-
r
L-phenylalanine amide
-
Glutamicibacter nicotianae D-phenylalanine amide
-
r
L-phenylalanine amide
-
Achromobacter obae D-phenylalanine amide
-
r
L-phenylalanine amide
-
Sinorhizobium medicae D-phenylalanine amide
-
r
L-phenylalanine amide
-
Sinorhizobium meliloti D-phenylalanine amide
-
r
L-phenylalanine amide
-
Janibacter sp. HTCC2649 D-phenylalanine amide
-
r
L-phenylalanine amide
-
Mesorhizobium opportunistum D-phenylalanine amide
-
r
L-phenylalanine amide
-
Mycolicibacterium vanbaalenii D-phenylalanine amide
-
r
L-phenylalanine amide
-
Brucella anthropi D-phenylalanine amide
-
r
L-phenylalanine amide
-
Citreicella sp. SE45 D-phenylalanine amide
-
r
L-phenylglycine amide
-
Glutamicibacter nicotianae D-phenylglycine amide
-
r
L-phenylglycine amide
-
Achromobacter obae D-phenylglycine amide
-
r
L-phenylglycine amide
-
Sinorhizobium medicae D-phenylglycine amide
-
r
L-phenylglycine amide
-
Sinorhizobium meliloti D-phenylglycine amide
-
r
L-phenylglycine amide
-
Janibacter sp. HTCC2649 D-phenylglycine amide
-
r
L-phenylglycine amide
-
Mesorhizobium opportunistum D-phenylglycine amide
-
r
L-phenylglycine amide
-
Mycolicibacterium vanbaalenii D-phenylglycine amide
-
r
L-phenylglycine amide
-
Brucella anthropi D-phenylglycine amide
-
r
L-phenylglycine amide
-
Citreicella sp. SE45 D-phenylglycine amide
-
r
L-serine amide
-
Glutamicibacter nicotianae D-serine amide
-
r
L-serine amide
-
Achromobacter obae D-serine amide
-
r
L-serine amide
-
Sinorhizobium medicae D-serine amide
-
r
L-serine amide
-
Sinorhizobium meliloti D-serine amide
-
r
L-serine amide
-
Janibacter sp. HTCC2649 D-serine amide
-
r
L-serine amide
-
Mesorhizobium opportunistum D-serine amide
-
r
L-serine amide
-
Brucella anthropi D-serine amide
-
r
L-serine amide
-
Citreicella sp. SE45 D-serine amide
-
r
L-tyrosine amide
-
Glutamicibacter nicotianae D-tyrosine amide
-
r
L-tyrosine amide
-
Sinorhizobium medicae D-tyrosine amide
-
r
L-tyrosine amide
-
Mesorhizobium opportunistum D-tyrosine amide
-
r
L-tyrosine amide
-
Sinorhizobium meliloti D-tyrosine amide
-
r
L-tyrosine amide
-
Brucella anthropi D-tyrosine amide
-
r
L-valine amide
-
Glutamicibacter nicotianae D-valine amide
-
r
L-valine amide
-
Achromobacter obae D-valine amide
-
r
L-valine amide
-
Sinorhizobium medicae D-valine amide
-
r
L-valine amide
-
Sinorhizobium meliloti D-valine amide
-
r
L-valine amide
-
Janibacter sp. HTCC2649 D-valine amide
-
r
L-valine amide
-
Mesorhizobium opportunistum D-valine amide
-
r
L-valine amide
-
Mycolicibacterium vanbaalenii D-valine amide
-
r
L-valine amide
-
Brucella anthropi D-valine amide
-
r
L-valine amide
-
Citreicella sp. SE45 D-valine amide
-
r
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?

Synonyms

Synonyms Comment Organism
ACL racemase
-
Glutamicibacter nicotianae
ACL racemase
-
Achromobacter obae
ACL racemase
-
Sinorhizobium medicae
ACL racemase
-
Sinorhizobium meliloti
ACL racemase
-
Janibacter sp. HTCC2649
ACL racemase
-
Mesorhizobium opportunistum
ACL racemase
-
Mycolicibacterium vanbaalenii
ACL racemase
-
Brucella anthropi
ACL racemase
-
Citreicella sp. SE45
More cf. EC 5.1.1.15 Glutamicibacter nicotianae
More cf. EC 5.1.1.15 Achromobacter obae
More cf. EC 5.1.1.15 Sinorhizobium medicae
More cf. EC 5.1.1.15 Sinorhizobium meliloti
More cf. EC 5.1.1.15 Janibacter sp. HTCC2649
More cf. EC 5.1.1.15 Mesorhizobium opportunistum
More cf. EC 5.1.1.15 Mycolicibacterium vanbaalenii
More cf. EC 5.1.1.15 Brucella anthropi
More cf. EC 5.1.1.15 Citreicella sp. SE45

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Glutamicibacter nicotianae
30
-
assay at Achromobacter obae
30
-
assay at Sinorhizobium medicae
30
-
assay at Sinorhizobium meliloti
30
-
assay at Janibacter sp. HTCC2649
30
-
assay at Mesorhizobium opportunistum
30
-
assay at Mycolicibacterium vanbaalenii
30
-
assay at Brucella anthropi
30
-
assay at Citreicella sp. SE45

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Glutamicibacter nicotianae
7
-
assay at Achromobacter obae
7
-
assay at Sinorhizobium medicae
7
-
assay at Sinorhizobium meliloti
7
-
assay at Janibacter sp. HTCC2649
7
-
assay at Mesorhizobium opportunistum
7
-
assay at Mycolicibacterium vanbaalenii
7
-
assay at Brucella anthropi
7.5
-
assay at Citreicella sp. SE45
8
-
assay at Brucella anthropi

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate PLP, the enzyme is a fold-type I PLP-dependent enzyme Achromobacter obae

General Information

General Information Comment Organism
evolution the enzyme belongs to the fold-type I PLP-dependent enzyme family Achromobacter obae
malfunction the mutation of either Asp210 or Lys267 to alanine abolish the racemization activity for 2-aminohexano-6-lactam Achromobacter obae
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