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Information on EC 5.1.1.15 - 2-aminohexano-6-lactam racemase
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EC Tree
5.1.1.15 2-aminohexano-6-lactam racemaseIUBMB Comments
Contains pyridoxal 5'-phosphate. Also racemises 2-aminopentano-5-lactam (alpha-amino-delta-valerolactam) and 2-amino-4-thiahexano-6-lactam (where S replaces CH2 of C-4). It does not catalyse the racemisation of alpha-amino acids but has some transaminase activity with them.
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Word Map
- 5.1.1.15
- synthesis
- amide
-
racemization
- 5'-phosphate
-
ochrobactrum
- anthropi
- pyridoxal
- d-aminopeptidase
The enzyme appears in viruses and cellular organisms
Synonyms
ACL racemase, ACLR, alpha-Amino-delta-valerolactam racemase, alpha-Amino-epsilon-caprolactam racemase, Aminocaprolactam racemase, moe, More, Racemase, alpha-amino-epsilon-caprolactam, Racemase, alpha-amino-epsilon-caprolactam (Achromobacter obae reduced), SMc02413, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ACL racemase
ACLR
alpha-Amino-delta-valerolactam racemase
-
-
-
-
alpha-Amino-epsilon-caprolactam racemase
Aminocaprolactam racemase
-
-
-
-
moe
Racemase, alpha-amino-epsilon-caprolactam
-
-
-
-
Racemase, alpha-amino-epsilon-caprolactam (Achromobacter obae reduced)
-
-
-
-
additional information
ACL racemase
-
-
-
-
alpha-Amino-epsilon-caprolactam racemase
-
-
-
-
alpha-Amino-epsilon-caprolactam racemase
Ochrobactrum anthropi ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168
-
-
additional information
Ochrobactrum anthropi ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168
cf. EC 5.1.1.10
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-2-aminohexano-6-lactam = (R)-2-aminohexano-6-lactam
-
-
-
-
(S)-2-aminohexano-6-lactam = (R)-2-aminohexano-6-lactam
single base mechanism
-
(S)-2-aminohexano-6-lactam = (R)-2-aminohexano-6-lactam
D- and L-amino acids are produced from L- and D-amino acid amides by D-aminopeptidase from Ochrobactrum anthropi C1-38 and L-amino acid amidase from Pseudomonas azotoformans IAM 1603, respectively, in the presence of alpha-amino-epsilon-caprolactam racemase from Achromobacter obae. Substrate: L-alanine amide, product: D-alanine (100% yield), substrate: L-2-aminobutyric amide, product: D-2-aminobutyric acid (100% yield), substrate: L-serine amide, product: D-serine (94% yield), substrate: L-methionine amide, product: D-methionine (100% yield), substrate: D-alanine amide, product: L-alanine (100% yield), substrate: D-leucine amide, product: L-leucine (100% yield), substrate: D-methionine amide, product: L-methionine (100% yield)
-
(S)-2-aminohexano-6-lactam = (R)-2-aminohexano-6-lactam
the racemization of ACL racemase proceeds via a two-base mechanism
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
2-aminohexano-6-lactam racemase
Contains pyridoxal 5'-phosphate. Also racemises 2-aminopentano-5-lactam (alpha-amino-delta-valerolactam) and 2-amino-4-thiahexano-6-lactam (where S replaces CH2 of C-4). It does not catalyse the racemisation of alpha-amino acids but has some transaminase activity with them.
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CAS REGISTRY NUMBER
COMMENTARY
120669-89-8
racemase, alpha-amino-epsilon-caprolactam (Achromobacter obae reduced)
52652-64-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-2-amino-delta-valerolactam
L-2-amino-delta-valerolactam
-
best substrate
-
-
r
D-2-amino-omega-octalactam
L-2-amino-omega-octalactam
-
1.78% activity compared to D-2-aminohexano-6-lactam
-
-
r
D-2-aminobutyric acid amide
L-2-aminobutyric acid amide
-
0.19% activity compared to D-2-aminohexano-6-lactam
-
-
r
D-alanine amide
L-alanine amide
-
2.12% activity compared to D-2-aminohexano-6-lactam
-
-
r
L-2-amino-delta-valerolactam
D-2-amino-delta-valerolactam
-
17.2% activity compared to D-2-aminohexano-6-lactam
-
-
r
L-2-amino-omega-octalactam
D-2-amino-omega-octalactam
-
1.41% activity compared to D-2-aminohexano-6-lactam
-
-
r
L-alpha-Amino-beta-thio-epsilon-caprolactam
D-alpha-Amino-beta-thio-epsilon-caprolactam
-
racemized more than 3times faster and binds about 4fold stronger to the enzyme than L-alpha-amino-epsilon-caprolactam
-
-
-
L-alpha-Amino-delta-valerolactam
D-alpha-Amino-delta-valerolactam
-
-
-
-
D-2-aminohexano-6-lactam
L-2-aminohexano-6-lactam
-
preferred substrate
-
-
r
D-2-aminohexano-6-lactam
L-2-aminohexano-6-lactam
-
preferred substrate
-
-
r
D-2-aminohexano-6-lactam
L-2-aminohexano-6-lactam
-
-
-
r
D-2-aminohexano-6-lactam
L-2-aminohexano-6-lactam
-
-
-
r
L-2-aminobutyric acid amide
D-2-aminobutyric acid amide
-
0.08% activity compared to D-2-aminohexano-6-lactam
-
-
r
L-2-aminohexano-6-lactam
D-2-aminohexano-6-lactam
-
-
-
r
L-2-aminohexano-6-lactam
D-2-aminohexano-6-lactam
-
-
-
r
L-alanine amide
D-alanine amide
-
0.77% activity compared to D-2-aminohexano-6-lactam
-
-
r
L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
-
-
-
-
L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
-
-
-
-
L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
-
-
-
-
L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
-
-
-
-
L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
-
-
-
-
L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
-
-
-
-
?
L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
-
-
-
r
L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
-
r
-
-
L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
-
r
-
-
L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
-
r
-
-
L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
-
-
-
-
L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
-
-
-
-
additional information
?
-
-
the enzyme catalyzes alpha-proton exchange of the substrate with deuterium during racemization in deuterium oxide
-
-
-
additional information
?
-
-
no racemization activity is observed with dipeptides or amino acid derivatives, such as L-Ala-D-Ala, D-Ala-L-Ala, L-alanylglycine, L-phenylglycine, or L-alanine methylester
-
-
-
additional information
?
-
-
The enzyme acts on a broad range of amino acid amides, particularly unbranched amino acid amides including L-alanine amide and L-serine amide. No activity with L-tyrosine amide
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
additional information
?
-
-
The enzyme acts on a broad range of amino acid amides, particularly unbranched amino acid amides including L-alanine amide and L-serine amide. No activity with L-tyrosine amide
-
-
-
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
-
-
-
additional information
?
-
-
the enzyme acts on 2-aminohexano-6-lactam and 2-amino acid amides, the enzyme prefers the D-enantiomers as substrates
-
-
-
additional information
?
-
-
the enzyme encoded by gene CQ758817 shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
-
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
-
-
-
additional information
?
-
Janibacter sp. HTCC 2649
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
?
-
Janibacter sp. HTCC 2649
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
additional information
?
-
Ochrobactrum 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
?
-
Ochrobactrum anthropi IA / NCBIMB41129
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
-
-
-
r
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
-
-
-
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
-
-
-
additional information
?
-
-
the enzyme encoded by gene CQ758817 shows enhanced alpha-amino-epsilon-caprolactam racemase activity on D- and L-2-aminohexano-6-lactams
-
-
-
additional information
?
-
Janibacter sp. HTCC 2649
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
?
-
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
?
-
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
?
-
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
?
-
-
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
?
-
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
?
-
-
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
?
-
Ochrobactrum 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
?
-
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
?
-
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
?
-
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
?
-
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
?
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
enzyme contains 1 mol of pyridoxal 5'-phosphate per mol of enzyme. Km: 0.00021 mM
pyridoxal 5'-phosphate
-
PLP, the enzyme is a fold-type I PLP-dependent enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-alpha-Amino-delta-valerolactam
-
inactivation is due to conversion of the enzyme-bound pyridoxal 5'-phosphate into pyridoxamine 5'-phosphate by transamination with L-alpha-amino-delta-valerolactam
additional information
-
racemization activity can partially be recovered by the subsequent addition of 1.0 mM pyridoxal 5'-phosphate
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.04
-
purified recombinant enzyme, substrate L-valine amide, pH 7.5, 30°C
0.06
-
purified recombinant enzyme, substrate L-valine amide, pH 7.5, 30°C
0.1
0.2
-
purified recombinant enzyme, substrate L-phenylalanine, pH 7.5, 30°C
0.3
-
purified recombinant enzyme, substrate L-phenylalanine, pH 7.5, 30°C
0.8
-
purified recombinant enzyme, substrate L-methionine amide, pH 7.5, 30°C
0.9
-
purified recombinant enzyme, substrate L-methionine amide, pH 7.5, 30°C
1.5
-
purified recombinant enzyme, substrate L-leucine amide, pH 7.5, 30°C
1.8
-
purified recombinant enzyme, substrate L-leucine amide, pH 7.5, 30°C
105
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C
107
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C
1072
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C
11
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C
1225
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 8.0, 30°C
133
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C
16.7
-
purified recombinant enzyme, substrate L-alanine amide, pH 7.5, 30°C
17.5
-
purified recombinant enzyme, substrate L-alanine amide, pH 7.5, 30°C
182
-
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C
20
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C
21.6
-
purified recombinant enzyme, substrate L-serine amide, pH 7.5, 30°C
260
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C
365
-
purified recombinant His-tagged enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C
39
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C
422
-
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C
443
444
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 8.0, 30°C
5.3
-
crude recombinant enzyme, substrate L-2-aminohexano-6-lactam, pH 7.5, 30°C
520
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C
627
63
68
purified enzyme, substrate L-2-aminohexano-6-lactam, pH 7.0, 30°C
681
772
94
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C
additional information
-
300 U/liter culture; the effect of the concentration of L-alanine amide on the racemization reaction catalyzed by ACL racemase is investigated. Formation of D-alanine amide increases when the concentration of L-alanine amide is increased from 0.6 M to 1.2 M, indicating that the enzyme activity is not inhibited by the high substrate concentration
0.1
-
purified recombinant enzyme, substrate L-phenylglycine, pH 7.5, 30°C
0.1
-
purified recombinant enzyme, substrate L-phenylglycine, pH 7.5, 30°C
63
purified enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C
681
-
purified recombinant enzyme, substrate L-2-aminohexano-6-lactam, pH 7.5, 30°C
772
-
purified recombinant enzyme, substrate D-2-aminohexano-6-lactam, pH 7.5, 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
7.5
8.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 12
-
active in a broad pH range, with more than 80 % activity in the pH range of pH 7.5-11.0, maximal activity at pH 10.0
6 - 8
-
pH 6.0: about 60% of maximal activity, pH 8.0: about 50% of maximal activity, L-alpha-amino-delta-valerolactam
6 - 9.5
-
pH 6.0: about 40% of maximal activity, pH 9.5: about 60% of maximal activity, L-alpha-amino-beta-thio-epsilon-caprolactam
6.5 - 9.2
-
the effect of pH on D- or L-alanine production from L- or D-alanine amide with D-aminopeptidase or L-Aminoacid amide hydrolase in the presence of ACL racemase is investigated. Racemization is performed by ACL racemase at pH values of 6.5 to 9.2, and the maximum rate of conversion is found at pH 7.5 and at a temperature of around 45°C
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 90
-
recombinant enzyme, activity range, enzyme activity rapidly increases between 40°C and 60°C and reaches its maximum at 70°C, above 70°C, the enzyme activity declines
30 - 95
-
50% of maximal activity at 30°C, about 40% at 90°C, and 20% at 95°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
-
the mutation of either Asp210 or Lys267 to alanine abolish the racemization activity for 2-aminohexano-6-lactam
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
evolution
-
the enzyme belongs to the fold-type I PLP-dependent enzyme family
evolution
-
the deduced amino acid sequence of ACLR from Ensifer sp. 23-3 exhibits high similarity (99%) to that of aspartate aminotransferase family protein (UniProt ID W8HW01) from Ensifer adhaerens strain OV14
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
A0A2S6R8Q6_9PROT
419
0
43530
TrEMBL
A0A2S6SAQ6_9PROT
439
0
47982
TrEMBL
A0A2S6R7Z9_9PROT
438
0
45858
TrEMBL
A0A2S6SW96_9PROT
439
0
47982
TrEMBL
A1T974_MYCVP
Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / NRRL B-24157 / PYR-1)
435
0
44405
TrEMBL
A6X7I5_OCHA4
Ochrobactrum anthropi (strain ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168)
436
0
46013
TrEMBL
F7Y223_MESOW
Mesorhizobium opportunistum (strain LMG 24607 / HAMBI 3007 / WSM2075)
438
0
46259
TrEMBL
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
at 20°C using the hanging-drop vapor diffusion method, crystal structures of native and epsilon-caprolactam complexed ACLR are solved at 2.21 and 2.40 Å indicating the catalytic residue as Tyr137
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
-
purified recombinant enzyme, 30°C, 30 min, about 60% activity remaining
748352
5.5 - 9
-
purified recombinant enzyme, 30°C, 30 min, over 80% activity remaining
748352
6 - 10
-
purified recombinant His-tagged enzyme, highly stable after 1 h incubation at 4°C, not stable under acidic conditions
748354
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 60
-
purified recombinant enzyme, pH 7.0, 30 min, 90% and more activity remaining
50
-
purified recombinant His-tagged enzyme, the enzyme retains more than 90% of its activity after being incubated at 50°C for 50 min, and enzyme activity significantly decreases at temperatures greater than 50°C
65
70
75
80
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing inactivates, particularly in dilute solution of less than 1 mg/ml
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.25 M sucrose, 10 mM potassium phosphate buffer, pH 7.3, 0.02 mM pyridoxal 5'-phosphate, 0.01% 2-mercaptoethanol, protein concentration: more than 0.3%, stable for at least 6 months
-
-20°C, 0.25 M sucrose, enzyme concentration above 3 mg protein/ml, stable for at least 6 months
-
20°C, 0.25 M sucrose, enzyme retains approximately 90% of its initial activity after storage for 4 months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme by several steps of ion exchange and hydrophobic interaction chromatography, dialysis, ultrafiltration, and gel filtration, recombinant His-tagged enzyme 31.9fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to homogeneity
-
recombinant His-tagged enzyme 129fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
-
recombinant His-tagged enzyme 27.9fold from Escherichia coli strain BL21(DE3) by heat treatment, nickel affinity chromatography, and dialysis
-
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis; recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis
using Ni Sepharose highperformance (Amersham) and anion-exchange chromatography (HiTrapQFF)
-
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis
-
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis
-
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis
-
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis
Janibacter sp. HTCC 2649
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis; recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis; recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ACL racemase from Achromobacter obae is expressed in Escherichia coli, 300 U/liter culture
-
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene ABI14443, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109; 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
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
gene ACLR, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109
-
gene CSE45_2055, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain JM109
gene CSE45_2055, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109
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. HTCC 2649
gene Mesop_2670, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109
gene Mvan_2918, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109
gene SM0020_01805, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109; gene SMc02413, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109
gene CSE45_2055, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain JM109
-
gene CSE45_2055, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain JM109
-
gene CSE45_2055, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109
-
gene CSE45_2055, sequence comparisons, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
Achromobacter obae which produces alpha-amino-epsilon-caprolactam racemase, is utilized in industry to produce L-Lys from DL-alpha-amino-epsilon-caprolactam with a high yield in the presence of Cryptococcus laurentii, an L-alpha-amino-epsilon caprolactamase producing yeast
synthesis
-
production of DL-alpha-amino-beta-caprolactam as nutrient and food supplement
synthesis
-
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
synthesis
-
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
synthesis
-
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
synthesis
Janibacter sp. HTCC 2649
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
synthesis
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
synthesis
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
synthesis
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production; the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
synthesis
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
synthesis
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production; the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
synthesis
Glutamicibacter nicotianae NCIMB 41126
-
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
-
synthesis
-
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
-
synthesis
-
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
-
synthesis
Ochrobactrum anthropi ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168
-
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
-
synthesis
Ochrobactrum anthropi IA / NCBIMB41129
-
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
-
synthesis
-
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
-
synthesis
-
the enzyme might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ahmed, S.A.; Esaki, N.; Tanaka, H.; Soda, K.
Mechanism of alpha-amino-epsilon-caprolactam racemase reaction
Biochemistry
25
385-388
1986
Achromobacter obae
brenda
Ahmed, S.A.; Esaki, N.; Tanaka, H.; Soda, K.
L-alpha-Amino-beta-thio-epsilon-caprolactam, a new sulfur-containing substrate for alpha-amino-epsilon-caprolactam racemase
FEBS Lett.
174
76-79
1984
Achromobacter obae
-
brenda
Ahmed, S.A.; Esaki, N.; Soda, K.
Purification and properties of alpha-amino-epsilon-caprolactam racemase from Achromobacter obae
FEBS Lett.
150
370-374
1982
Achromobacter obae, Achromobacter obae FERM-P776
brenda
Ahmed, S.A.; Esaki, N.; Tanaka, H.; Soda, K.
Mechanism of inactivation of alpha-amino-epsilon-caprolactam racemase by alpha-amino-delta-valerolactam
Agric. Biol. Chem.
49
2991-2997
1985
Achromobacter obae
-
brenda
Ahmed, S.A.; Esaki, N.; Tanaka, H.; Soda, K.
Properties of alpha-amino-epsilon-caprolactam racemase from Achromobacter obae
Agric. Biol. Chem.
47
1887-1893
1983
Achromobacter obae
-
brenda
Ahmed, S.A.; Esaki, N.; Tanaka, H.; Soda, K.
Racemization of alpha-amino-delta-valerolactam catalyzed by alpha-amino-epsilon-caprolactam racemase from Achromobacter obae
Agric. Biol. Chem.
47
1149-1150
1983
Achromobacter obae
-
brenda
Fukumura, T.
Partial purification and some properties of alpha-amino-epsilon-caprolactam-racemizing enzyme from Achromobacter obae
Agric. Biol. Chem.
41
1509-1510
1977
Achromobacter obae
-
brenda
Plhackova, K.; Vojtisek, V.; Plachy, J.
Enzymic synthesis of L-lysine from DL-alpha-amino-epsilon-caprolactam by new microbial strains
Folia Microbiol. (Praha)
27
382-389
1982
Pseudomonas sp., Pseudomonas sp. CCM 3443
brenda
Crosby, J.
Synthesis of optically active compounds: A large scale perspective
Tetrahedron
47
4789-4846
1991
Achromobacter obae
-
brenda
Asano, Y.; Yamaguchi, S.
Dynamic kinetic resolution of amino acid amide catalyzed by D-aminopeptidase and alpha-amino-epsilon-caprolactam racemase
J. Am. Chem. Soc.
127
7696-7697
2005
Achromobacter obae
brenda
Yamaguchi, S.; Komeda, H.; Asano, Y.
New enzymatic method of chiral amino acid synthesis by dynamic kinetic resolution of amino acid amides: use of stereoselective amino acid amidases in the presence of alpha-amino-epsilon-caprolactam racemase
Appl. Environ. Microbiol.
73
5370-5373
2007
Achromobacter obae
brenda
Okazaki, S.; Suzuki, A.; Mizushima, T.; Kawano, T.; Komeda, H.; Asano, Y.; Yamane, T.
The novel structure of a pyridoxal 5-phosphate-dependent fold-type I racemase, alpha-amino-epsilon-caprolactam racemase from Achromobacter obae
Biochemistry
48
941-950
2009
Achromobacter obae (Q7M181)
brenda
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
Appl. Biochem. Biotechnol.
176
1303-1314
2015
Achromobacter obae (Q7M181), Citreicella sp. SE45, Glutamicibacter nicotianae, Glutamicibacter nicotianae NCIMB 41126, Janibacter sp. HTCC 2649 (A3TM80), Mesorhizobium opportunistum (F7Y223), Mesorhizobium opportunistum WSM 2075 (F7Y223), Mycolicibacterium vanbaalenii (A1T974), Mycolicibacterium vanbaalenii PYR-1 (A1T974), Ochrobactrum anthropi (A6X7I5), Ochrobactrum anthropi, Ochrobactrum anthropi ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168 (A6X7I5), Ochrobactrum anthropi IA / NCBIMB41129, Sinorhizobium medicae (A6UKD1), Sinorhizobium medicae WSM 419 (A6UKD1), Sinorhizobium meliloti (H0FT96), Sinorhizobium meliloti (Q92MM4), Sinorhizobium meliloti CCNWSX0020 (H0FT96)
brenda
Matsui, D.; Fuhshuku, K.I.; Nagamori, S.; Takata, M.; Asano, Y.
Isolation and characterization of racemase from Ensifer sp. 23-3 that acts on alpha-aminolactams and alpha-amino acid amides
J. Ind. Microbiol. Biotechnol.
44
1503-1510
2017
Ensifer sp. 23-3
brenda
Payoungkiattikun, W.; Okazaki, S.; Ina, A.; H-Kittikun, A.; Asano, Y.
Characterization of an alpha-amino-epsilon-caprolactam racemase with broad substrate specificity from Citreicella sp. SE45
J. Ind. Microbiol. Biotechnol.
44
677-685
2017
Achromobacter obae (Q7M181), Citreicella sp. SE45
brenda
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