Literature summary for 5.1.1.15 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 .

Application

Application	Comment	Organism
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	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	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.
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	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

Organism	UniProt	Comment	Textmining
Achromobacter obae	Q7M181	-	-
Brucella anthropi	-	-	-
Brucella anthropi	A6X7I5	-	-
Brucella anthropi ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168	A6X7I5	-	-
Brucella anthropi IA / NCBIMB41129	-	-	-
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	Brucella anthropi
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	Citreicella sp. SE45

Reaction

Reaction	Comment	Organism	Reaction ID
(S)-2-aminohexano-6-lactam = (R)-2-aminohexano-6-lactam	the racemization of ACL racemase proceeds via a two-base mechanism	Achromobacter obae	a

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.
D-2-aminohexano-6-lactam	-	Brucella anthropi	L-2-aminohexano-6-lactam	-	r
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	-	Citreicella sp. SE45	L-2-aminohexano-6-lactam	-	r
D-2-aminohexano-6-lactam	-	Brucella anthropi IA / NCBIMB41129	L-2-aminohexano-6-lactam	-	r
L-2-aminohexano-6-lactam	-	Brucella anthropi	D-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	-	Citreicella sp. SE45	D-2-aminohexano-6-lactam	-	r
L-2-aminohexano-6-lactam	-	Brucella anthropi IA / NCBIMB41129	D-2-aminohexano-6-lactam	-	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 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	?	-	?
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	?	-	?
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	?	-	?
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	?	-	?
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	?	-	?
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	?	-	?
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	?	-	?
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	?	-	?
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	?	-	?
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	?	-	?
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	?	-	?
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 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

Synonyms	Comment	Organism
ACL racemase	-	Brucella anthropi
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	-	Citreicella sp. SE45
alpha-Amino-epsilon-caprolactam racemase	-	Brucella anthropi
alpha-Amino-epsilon-caprolactam racemase	-	Glutamicibacter nicotianae
alpha-Amino-epsilon-caprolactam racemase	-	Achromobacter obae
alpha-Amino-epsilon-caprolactam racemase	-	Sinorhizobium medicae
alpha-Amino-epsilon-caprolactam racemase	-	Sinorhizobium meliloti
alpha-Amino-epsilon-caprolactam racemase	-	Janibacter sp. HTCC2649
alpha-Amino-epsilon-caprolactam racemase	-	Mesorhizobium opportunistum
alpha-Amino-epsilon-caprolactam racemase	-	Mycolicibacterium vanbaalenii
alpha-Amino-epsilon-caprolactam racemase	-	Citreicella sp. SE45
moe	cf. EC 5.1.1.10	Sinorhizobium medicae
More	cf. EC 5.1.1.10	Brucella anthropi
More	cf. EC 5.1.1.10	Glutamicibacter nicotianae
More	cf. EC 5.1.1.10	Achromobacter obae
More	cf. EC 5.1.1.10	Sinorhizobium meliloti
More	cf. EC 5.1.1.10	Janibacter sp. HTCC2649
More	cf. EC 5.1.1.10	Mesorhizobium opportunistum
More	cf. EC 5.1.1.10	Mycolicibacterium vanbaalenii
More	cf. EC 5.1.1.10	Citreicella sp. SE45
SMc02413	-	Sinorhizobium meliloti

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	assay at	Brucella anthropi
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	Citreicella sp. SE45

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7	-	assay at	Brucella anthropi
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
7.5	-	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