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Literature summary extracted from

  • Cao, Y.; Han, S.; Yu, L.; Qian, H.; Chen, J.Z.
    MD and QM/MM studies on long-chain L-alpha-hydroxy acid oxidase substrate binding features and oxidation mechanism (2014), J. Phys. Chem. B, 118, 5406-5417 .
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.3.15 analysis of the crystal structure of enzyme LCHAO in complex with cofactor FMN and inhibitor 4-carboxy-5-[(4-chlorophenyl)sulfanyl]-1,2,3-thiadiazole (CCPST) at 1.3 A resolution Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
1.1.3.15 Y129F site-directed mutagenesis of the key active site residue, the mutant enzymes shows highly reduced kcat but unaltered Km value compared to wild-type enzyme, modeling of the hydride transfer of mutant enzyme with bound FMN and lactate, the missing H-bond changes the mechanism of the LCHAO Y129F mutant catalyzed oxidation reaction Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.3.15 4-carboxy-5-[(4-chlorophenyl)sulfanyl]-1,2,3-thiadiazole CCPST Rattus norvegicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.3.15 (S)-lactate + O2 Rattus norvegicus
-
 pyruvate + H2O2
-
 ?
1.1.3.15 an (S)-2-hydroxy carboxylate + O2 Rattus norvegicus
-
 a 2-oxo carboxylate + H2O2
-
 ?
1.1.3.15 additional information Rattus norvegicus long-chain L-alpha-hydroxy acid oxidase (LCHAO) is a FMN-dependent oxidase that dehydrogenates L-alpha-hydroxy acids to oxo acids ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.15 Rattus norvegicus Q07523
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.3.15 an (S)-2-hydroxy carboxylate + O2 = a 2-oxo carboxylate + H2O2 reaction mechanism, quantum mechanics/molecular mechanics calculations and molecular dynamics simulations, overview. LCHAO-catalyzed dehydrogenation of L-lactate is a stepwise catalytic reaction in a hydride transfer mechanism but not a carbanion mechanism. In contrast to the wild-type enzyme, the mutant Y129F LCHAO catalyzes the oxidation of L-lactate in one step Rattus norvegicus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.15 (S)-lactate + O2
-
 Rattus norvegicus pyruvate + H2O2
-
 ?
1.1.3.15 an (S)-2-hydroxy carboxylate + O2
-
 Rattus norvegicus a 2-oxo carboxylate + H2O2
-
 ?
1.1.3.15 additional information long-chain L-alpha-hydroxy acid oxidase (LCHAO) is a FMN-dependent oxidase that dehydrogenates L-alpha-hydroxy acids to oxo acids Rattus norvegicus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.3.15 Hao2
-
 Rattus norvegicus
1.1.3.15 LCHAO
-
 Rattus norvegicus
1.1.3.15 long-chain L-alpha-hydroxy acid oxidase
-
 Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.15 FMN dependent on Rattus norvegicus

General Information

EC Number General Information Comment Organism
1.1.3.15 evolution the enzyme belongs to the family of L-2-hydroxy acid oxidases Rattus norvegicus
1.1.3.15 additional information the key residue Tyr129 in the active site of LCHAO does affect L-lactate binding to LCHAO but plays an important role on the catalytic reaction process through an H-bond interaction. Generation of a structural model of LCHAO-FMN-lactate. The active site informed by residues Phe23, Tyr129, Asp157, Arg164, Lys223, His247, and Arg250 Rattus norvegicus