Information on EC 5.1.1.15 - 2-aminohexano-6-lactam racemase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
5.1.1.15
-
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RECOMMENDED NAME
GeneOntology No.
2-aminohexano-6-lactam racemase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(S)-2-aminohexano-6-lactam = (R)-2-aminohexano-6-lactam
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
-
-
-
-
racemization
-
-
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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 hide
120669-89-8
racemase, alpha-amino-epsilon-caprolactam (Achromobacter obae reduced)
52652-64-9
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
FERM-P776
-
-
Manually annotated by BRENDA team
CCM 3443
-
-
Manually annotated by BRENDA team
CCM 3443
-
-
Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-Ala
L-Ala
show the reaction diagram
-
-
-
-
r
D-alpha-amino-beta-caprolactam
DL-alpha-amino-beta-caprolactam
show the reaction diagram
-
-
-
-
-
L-2-aminobutyric acid amide
D-2-aminobutyric acid amide
show the reaction diagram
-
-
-
-
r
L-alanine amide
D-alanine amide
show the reaction diagram
-
-
-
-
?
L-alpha-Amino-beta-thio-epsilon-caprolactam
D-alpha-Amino-beta-thio-epsilon-caprolactam
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
show the reaction diagram
additional information
?
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-alpha-Amino-epsilon-caprolactam
D-alpha-Amino-epsilon-caprolactam
show the reaction diagram
Q7M181
-
-
-
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Methyl-3-benzothiazolonehydrazone hydrochloride
-
-
D-alpha-Amino-delta-valerolactam
-
-
D-alpha-aminobutyrate
-
-
D-cycloserine
-
-
epsilon-Caprolactam
-
-
hydroxylamine
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
L-alpha-aminobutyrate
-
-
L-Phe
-
weak
L-Trp
-
weak
phenylhydrazine
-
-
Sodium borohydride
-
-
taurine
-
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.4
D-Ala
-
-
3.5 - 8
D-alpha-Amino-epsilon-caprolactam
1.1
L-2-aminobutyric acid amide
-
-
2.5
L-Ala
-
-
1.5
L-alpha-Amino-beta-thio-epsilon-caprolactam
-
-
2.9
L-alpha-Amino-delta-valerolactam
-
-
6 - 10
L-alpha-amino-epsilon-caprolactam
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
L-alpha-amino-delta-valerolactam
7.5
-
highest conversion
9
-
L-alpha-amino-epsilon-caprolactam
10
-
L-alpha-amino-beta-thio-epsilon-caprolactam
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
7 - 9.8
-
L-alpha-amino-beta-thio-epsilon-caprolactam
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
maximum conversion rate
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Achromobacter obae;
N6UXY4
Rhizobium freirei PRF 81;
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49000
-
1 * 49000, SDS-PAGE
51000
-
gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
6 - 9
-
at 25°C, 20 min, stable
2088
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
pH 7.2, 20 min, stable
65
-
pH 7.2, 20 min, 5% loss of activity
70
-
pH 7.2, 20 min, 15% loss of activity
75
-
pH 7.2, 20 min, 40% loss of activity
80
-
pH 7.2, 20 min, 25% loss of activity
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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
ACL racemase is purified from Escherichia coli JM109/pACL60
-
recombinant
-
using Ni Sepharose highperformance (Amersham) and anion-exchange chromatography (HiTrapQFF)
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ACL racemase from Achromobacter obae is expressed in Escherichia coli, 300 U/liter culture
-
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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LINKS TO OTHER DATABASES (specific for EC-Number 5.1.1.15)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)