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Literature summary extracted from

  • Awad, R.; Gans, P.; Reiser, J.B.
    Structural insights into the substrate recognition and reaction specificity of the PLP-dependent fold-type I isoleucine 2-epimerase from Lactobacillus buchneri (2017), Biochimie, 137, 165-173 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.1.1.21 recombinant expression of codon-optimized, His-tagged enzyme in Escherichia coli strain BL21(DE3) Lentilactobacillus buchneri

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.1.1.21 purified recombinant His-tagged enzyme alone or in complex with pyridoxal 5'-phosphate, hanging drop vapour diffusion technique, mixing of 0.002 ml of 2-8 mg/ml protein in 50 mM Na-phosphate, pH 7.2, and 0.1 mM 2-mercaptoethanol, with 0.002 ml of reservoir solution containing 12-18% PEG 3350 and 100 mM lithium citrate, 20°C, several weeks, for complex crystals soaking in pyridoxal 5'-phosphate containing mother liquor, X-ray diffraction structure determination and analysis at 2.6 A and 2.15 A resolution, respectively Lentilactobacillus buchneri

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.1.1.21 200000
-
recombinnat His-tagged enzyme, gel filtration Lentilactobacillus buchneri

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.1.1.21 L-isoleucine Lentilactobacillus buchneri
-
D-allo-isoleucine
-
r
5.1.1.21 L-isoleucine Lentilactobacillus buchneri JCM 1115
-
D-allo-isoleucine
-
r

Organism

EC Number Organism UniProt Comment Textmining
5.1.1.21 Lentilactobacillus buchneri M1GRN3
-
-
5.1.1.21 Lentilactobacillus buchneri JCM 1115 M1GRN3
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.1.1.21 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromtography and gel filtration Lentilactobacillus buchneri

Reaction

EC Number Reaction Comment Organism Reaction ID
5.1.1.21 L-isoleucine = D-allo-isoleucine the racemization reaction by the fold-type I racemases may generally occur thanks to a revised two-base mechanism. Conformational changes provoked by pyridoxal 5'-phosphate binding suggesting an induced fit of the active site entrance door necessary to accommodate pyridoxal 5'-phosphate and substrate molecules Lentilactobacillus buchneri

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.1.21 L-isoleucine
-
Lentilactobacillus buchneri D-allo-isoleucine
-
r
5.1.1.21 L-isoleucine
-
Lentilactobacillus buchneri JCM 1115 D-allo-isoleucine
-
r
5.1.1.21 additional information the enzyme catalyzes the pyridoxal 5'-phosphate (PLP)-dependent racemization and epimerization of a broad spectrum of nonpolar amino acids from L- to D-form and vice versa, in particular isoleucine Lentilactobacillus buchneri ?
-
?
5.1.1.21 additional information the enzyme catalyzes the pyridoxal 5'-phosphate (PLP)-dependent racemization and epimerization of a broad spectrum of nonpolar amino acids from L- to D-form and vice versa, in particular isoleucine Lentilactobacillus buchneri JCM 1115 ?
-
?

Synonyms

EC Number Synonyms Comment Organism
5.1.1.21 BCAA racemase UniProt Lentilactobacillus buchneri
5.1.1.21 isoleucine 2-epimerase
-
Lentilactobacillus buchneri
5.1.1.21 PLP-dependent fold-type I isoleucine 2-epimerase
-
Lentilactobacillus buchneri

Cofactor

EC Number Cofactor Comment Organism Structure
5.1.1.21 pyridoxal 5'-phosphate PLP, dependent on Lentilactobacillus buchneri

General Information

EC Number General Information Comment Organism
5.1.1.21 evolution the enzyme belongs to the fold-type I subgroup of pyridoxal 5'-phosphate-dependent enzymes and is very close to aminobutyrate aminotransferases family Lentilactobacillus buchneri
5.1.1.21 additional information identification of the active site residues responsible for its nonpolar amino acid recognition and reactivity specificity from structure comparisons with the alpha-amino-epsilon-caprolactam racemase (EC 5.1.1.15) from Achromobacter obae and the cystathionine beta-lyase (EC 4.4.1.8) from Escherichia coli (PDB IDs 2ZUK and 3DXW), active site structure, overview Lentilactobacillus buchneri