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Literature summary extracted from

  • 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 (2017), J. Ind. Microbiol. Biotechnol., 44, 1503-1510 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.1.1.15 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) Ensifer sp. 23-3

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.1.1.15 5,5'-dithiobis(2-nitrobenzoic acid) complete inhibition at 1 mM Ensifer sp. 23-3
5.1.1.15 8-hydroxyquinoline 59% inhibition at 1 mM Ensifer sp. 23-3
5.1.1.15 Ag+ 88% inhibition at 1 mM Ensifer sp. 23-3
5.1.1.15 Al3+ 57% inhibition at 1 mM Ensifer sp. 23-3
5.1.1.15 Cd2+ 57% inhibition at 1 mM Ensifer sp. 23-3
5.1.1.15 Co2+ 32% inhibition at 1 mM Ensifer sp. 23-3
5.1.1.15 Cr3+ 23% inhibition at 1 mM Ensifer sp. 23-3
5.1.1.15 Cu2+ complete inhibition at 1 mM Ensifer sp. 23-3
5.1.1.15 D-cycloserine 21% inhibition at 1 mM Ensifer sp. 23-3
5.1.1.15 D-penicillamine 88% inhibition at 1 mM Ensifer sp. 23-3
5.1.1.15 Hg2+ complete inhibition at 1 mM Ensifer sp. 23-3
5.1.1.15 hydroxylamine complete inhibition at 1 mM Ensifer sp. 23-3
5.1.1.15 iodoacetic acid 12% inhibition at 1 mM Ensifer sp. 23-3
5.1.1.15 Mn2+ 62% inhibition at 1 mM Ensifer sp. 23-3
5.1.1.15 additional information racemization activity can partially be recovered by the subsequent addition of 1.0 mM pyridoxal 5'-phosphate Ensifer sp. 23-3
5.1.1.15 N-ethylmaleimide 50% inhibition at 1 mM Ensifer sp. 23-3
5.1.1.15 Ni2+ 58% inhibition at 1 mM Ensifer sp. 23-3
5.1.1.15 phenylmethane sulfonyl fluoride 59% inhibition at 1 mM Ensifer sp. 23-3
5.1.1.15 Zn2+ 43% inhibition at 1 mM Ensifer sp. 23-3

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.1.1.15 1.3
-
 L-alanine amide recombinant enzyme, pH 7.0, 30°C Ensifer sp. 23-3
5.1.1.15 2.1
-
 L-2-aminobutyric acid amide recombinant enzyme, pH 7.0, 30°C Ensifer sp. 23-3
5.1.1.15 3.5
-
 D-2-Aminobutyric acid amide recombinant enzyme, pH 7.0, 30°C Ensifer sp. 23-3
5.1.1.15 3.8
-
 D-alanine amide recombinant enzyme, pH 7.0, 30°C Ensifer sp. 23-3
5.1.1.15 11.2
-
 L-2-aminohexano-6-lactam recombinant enzyme, pH 7.0, 30°C Ensifer sp. 23-3

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
5.1.1.15 cytoplasm
-
 Ensifer sp. 23-3 5737
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.1.1.15 49800
-
 native enzyme, gel filtration Ensifer sp. 23-3

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.1.1.15 D-2-aminohexano-6-lactam Ensifer sp. 23-3
-
 L-2-aminohexano-6-lactam
-
 r

Organism

EC Number Organism UniProt Comment Textmining
5.1.1.15 Ensifer sp. 23-3
-
 isolated from soil
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.1.1.15 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 Ensifer sp. 23-3

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.1.1.15 365
-
 purified recombinant His-tagged enzyme, substrate D-2-aminohexano-6-lactam, pH 7.0, 30°C Ensifer sp. 23-3

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.1.15 D-2-amino-delta-valerolactam best substrate Ensifer sp. 23-3 L-2-amino-delta-valerolactam
-
 r
5.1.1.15 D-2-amino-omega-octalactam 1.78% activity compared to D-2-aminohexano-6-lactam Ensifer sp. 23-3 L-2-amino-omega-octalactam
-
 r
5.1.1.15 D-2-aminobutyric acid amide 0.19% activity compared to D-2-aminohexano-6-lactam Ensifer sp. 23-3 L-2-aminobutyric acid amide
-
 r
5.1.1.15 D-2-aminohexano-6-lactam
-
 Ensifer sp. 23-3 L-2-aminohexano-6-lactam
-
 r
5.1.1.15 D-2-aminohexano-6-lactam high activity Ensifer sp. 23-3 L-2-aminohexano-6-lactam
-
 r
5.1.1.15 D-alanine amide 2.12% activity compared to D-2-aminohexano-6-lactam Ensifer sp. 23-3 L-alanine amide
-
 r
5.1.1.15 L-2-amino-delta-valerolactam 17.2% activity compared to D-2-aminohexano-6-lactam Ensifer sp. 23-3 D-2-amino-delta-valerolactam
-
 r
5.1.1.15 L-2-amino-omega-octalactam 1.41% activity compared to D-2-aminohexano-6-lactam Ensifer sp. 23-3 D-2-amino-omega-octalactam
-
 r
5.1.1.15 L-2-aminobutyric acid amide 0.08% activity compared to D-2-aminohexano-6-lactam Ensifer sp. 23-3 D-2-aminobutyric acid amide
-
 r
5.1.1.15 L-2-aminohexano-6-lactam high activity Ensifer sp. 23-3 D-2-aminohexano-6-lactam
-
 r
5.1.1.15 L-alanine amide 0.77% activity compared to D-2-aminohexano-6-lactam Ensifer sp. 23-3 D-alanine amide
-
 r
5.1.1.15 additional information the enzyme acts on 2-aminohexano-6-lactam and 2-amino acid amides, the enzyme prefers the D-enantiomers as substrates Ensifer sp. 23-3 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
5.1.1.15 monomer 1 * 45000, native enzyme, SDS-PAGE Ensifer sp. 23-3

Synonyms

EC Number Synonyms Comment Organism
5.1.1.15 ACL racemase
-
 Ensifer sp. 23-3
5.1.1.15 ACLR
-
 Ensifer sp. 23-3
5.1.1.15 alpha-Amino-epsilon-caprolactam racemase
-
 Ensifer sp. 23-3

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.1.1.15 65 70
-
 Ensifer sp. 23-3

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
5.1.1.15 30 95 50% of maximal activity at 30°C, about 40% at 90°C, and 20% at 95°C Ensifer sp. 23-3

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
5.1.1.15 30 60 purified recombinant enzyme, pH 7.0, 30 min, 90% and more activity remaining Ensifer sp. 23-3
5.1.1.15 65
-
 purified recombinant enzyme, pH 7.0, 30 min, 70% activity remaining Ensifer sp. 23-3
5.1.1.15 70
-
 purified recombinant enzyme, pH 7.0, 30 min, 30% activity remaining Ensifer sp. 23-3
5.1.1.15 75
-
 purified recombinant enzyme, pH 7.0, 30 min, 10% activity remaining Ensifer sp. 23-3
5.1.1.15 80
-
 purified recombinant enzyme, pH 7.0, 30 min, inactivation Ensifer sp. 23-3

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.1.1.15 0.7
-
 L-2-aminobutyric acid amide recombinant enzyme, pH 7.0, 30°C Ensifer sp. 23-3
5.1.1.15 1.1
-
 D-2-Aminobutyric acid amide recombinant enzyme, pH 7.0, 30°C Ensifer sp. 23-3
5.1.1.15 3.3
-
 L-alanine amide recombinant enzyme, pH 7.0, 30°C Ensifer sp. 23-3
5.1.1.15 10.2
-
 D-alanine amide recombinant enzyme, pH 7.0, 30°C Ensifer sp. 23-3
5.1.1.15 371
-
 L-2-aminohexano-6-lactam recombinant enzyme, pH 7.0, 30°C Ensifer sp. 23-3

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.1.1.15 8 9
-
 Ensifer sp. 23-3

pH Range

EC Number pH Minimum pH Maximum Comment Organism
5.1.1.15 5.5 10.5 over 50% of maximal activity Ensifer sp. 23-3

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
5.1.1.15 4.5
-
 purified recombinant enzyme, 30°C, 30 min, inactivation Ensifer sp. 23-3
5.1.1.15 5
-
 purified recombinant enzyme, 30°C, 30 min, about 60% activity remaining Ensifer sp. 23-3
5.1.1.15 5.5 9 purified recombinant enzyme, 30°C, 30 min, over 80% activity remaining Ensifer sp. 23-3
5.1.1.15 9
-
 purified recombinant enzyme, 30°C, 30 min, about 75% activity remaining Ensifer sp. 23-3
5.1.1.15 10
-
 purified recombinant enzyme, 30°C, 30 min, about 60% activity remaining Ensifer sp. 23-3
5.1.1.15 11
-
 purified recombinant enzyme, 30°C, 30 min, inactivation Ensifer sp. 23-3

Cofactor

EC Number Cofactor Comment Organism Structure
5.1.1.15 pyridoxal 5'-phosphate dependent on, may be tightly bound to the enzyme Ensifer sp. 23-3

General Information

EC Number General Information Comment Organism
5.1.1.15 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 Ensifer sp. 23-3

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
5.1.1.15 0.31
-
 D-2-Aminobutyric acid amide recombinant enzyme, pH 7.0, 30°C Ensifer sp. 23-3
5.1.1.15 0.33
-
 L-2-aminobutyric acid amide recombinant enzyme, pH 7.0, 30°C Ensifer sp. 23-3
5.1.1.15 2.54
-
 L-alanine amide recombinant enzyme, pH 7.0, 30°C Ensifer sp. 23-3
5.1.1.15 2.68
-
 D-alanine amide recombinant enzyme, pH 7.0, 30°C Ensifer sp. 23-3
5.1.1.15 33.1
-
 L-2-aminohexano-6-lactam recombinant enzyme, pH 7.0, 30°C Ensifer sp. 23-3