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Information on EC 5.1.1.15 - 2-aminohexano-6-lactam racemase for references in articles please use BRENDA:EC5.1.1.15Word Map on EC 5.1.1.15
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The enzyme appears in viruses and cellular organisms
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2-aminohexano-6-lactam racemase
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(S)-2-aminohexano-6-lactam = (R)-2-aminohexano-6-lactam
(S)-2-aminohexano-6-lactam = (R)-2-aminohexano-6-lactam
single base mechanism
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(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)
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(S)-2-aminohexano-6-lactam = (R)-2-aminohexano-6-lactam
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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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alpha-Amino-delta-valerolactam racemase
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alpha-Amino-epsilon-caprolactam racemase
Aminocaprolactam racemase
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Racemase, alpha-amino-epsilon-caprolactam
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Racemase, alpha-amino-epsilon-caprolactam (Achromobacter obae reduced)
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ACL racemase
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alpha-Amino-epsilon-caprolactam racemase
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alpha-Amino-epsilon-caprolactam racemase
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alpha-Amino-epsilon-caprolactam racemase
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120669-89-8
racemase, alpha-amino-epsilon-caprolactam (Achromobacter obae reduced)
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FERM-P776
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brenda
CCM 3443
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brenda
CCM 3443
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brenda
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brenda
-
UniProt
brenda
FERM-P776
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-
brenda
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D-alpha-amino-beta-caprolactam
DL-alpha-amino-beta-caprolactam
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-
-
-
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L-2-aminobutyric acid amide
D-2-aminobutyric acid amide
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-
-
-
r
L-alanine amide
D-alanine amide
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-
-
-
?
L-alpha-Amino-beta-thio-epsilon-caprolactam
D-alpha-Amino-beta-thio-epsilon-caprolactam
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racemized more than 3times faster and binds about 4fold stronger to the enzyme than L-alpha-amino-epsilon-caprolactam
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L-alpha-Amino-delta-valerolactam
D-alpha-Amino-delta-valerolactam
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L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
additional information
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L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
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-
-
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L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
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L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
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L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
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-
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L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
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-
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L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
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?
L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
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-
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r
L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
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r
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L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
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r
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L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
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r
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L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
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-
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L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
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-
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additional information
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the enzyme catalyzes alpha-proton exchange of the substrate with deuterium during racemization in deuterium oxide
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additional information
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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
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L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
Q7M181
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r
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pyridoxal 5'-phosphate
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enzyme contains 1 mol of pyridoxal 5'-phosphate per mol of enzyme. Km: 0.00021 mM
pyridoxal 5'-phosphate
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contains pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
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2-Methyl-3-benzothiazolonehydrazone hydrochloride
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D-alpha-Amino-delta-valerolactam
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D-alpha-aminobutyrate
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L-alpha-Amino-delta-valerolactam
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inactivation is due to conversion of the enzyme-bound pyridoxal 5'-phosphate into pyridoxamine 5'-phosphate by transamination with L-alpha-amino-delta-valerolactam
L-alpha-aminobutyrate
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-
hydroxylamine
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5 mM
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3.5 - 8
D-alpha-Amino-epsilon-caprolactam
1.1
L-2-aminobutyric acid amide
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-
1.5
L-alpha-Amino-beta-thio-epsilon-caprolactam
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-
2.9
L-alpha-Amino-delta-valerolactam
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6 - 10
L-alpha-amino-epsilon-caprolactam
3.5
D-alpha-Amino-epsilon-caprolactam
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8
D-alpha-Amino-epsilon-caprolactam
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6
L-alpha-amino-epsilon-caprolactam
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10
L-alpha-amino-epsilon-caprolactam
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additional information
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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
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7
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L-alpha-amino-delta-valerolactam
9
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L-alpha-amino-epsilon-caprolactam
10
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L-alpha-amino-beta-thio-epsilon-caprolactam
8.8
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L-alpha-amino-epsilon-caprolactam
8.8
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D-alpha-amino-epsilon-caprolactam; L-alpha-amino-epsilon-caprolactam
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6 - 8
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pH 6.0: about 60% of maximal activity, pH 8.0: about 50% of maximal activity, L-alpha-amino-delta-valerolactam
6 - 9.5
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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
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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
7 - 9.8
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L-alpha-amino-beta-thio-epsilon-caprolactam
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45
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maximum conversion rate
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brenda
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49000
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1 * 49000, SDS-PAGE
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monomer
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1 * 49000, SDS-PAGE
monomer
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1 * 49000, SDS-PAGE
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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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6 - 9
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at 25°C, 20 min, stable
2088
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60
-
pH 7.2, 20 min, stable
65
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pH 7.2, 20 min, 5% loss of activity
70
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pH 7.2, 20 min, 15% loss of activity
75
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pH 7.2, 20 min, 40% loss of activity
80
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pH 7.2, 20 min, 25% loss of activity
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freezing inactivates, particularly in dilute solution of less than 1 mg/ml
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-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
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-20°C, 0.25 M sucrose, enzyme concentration above 3 mg protein/ml, stable for at least 6 months
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20°C, 0.25 M sucrose, enzyme retains approximately 90% of its initial activity after storage for 4 months
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ACL racemase is purified from Escherichia coli JM109/pACL60
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using Ni Sepharose highperformance (Amersham) and anion-exchange chromatography (HiTrapQFF)
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ACL racemase from Achromobacter obae is expressed in Escherichia coli, 300 U/liter culture
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expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
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synthesis
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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
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production of DL-alpha-amino-beta-caprolactam as nutrient and food supplement
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ACLR_ACHOB
436
45699
Swiss-Prot
A0A2S6R7Z9_9PROT
438
45858
TrEMBL
A0A2S6R8Q6_9PROT
419
43530
TrEMBL
A0A2S6SW96_9PROT
439
47982
TrEMBL
N6UXY4_9RHIZ
436
45644
TrEMBL
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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, Achromobacter obae (Q7M181)
brenda
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