Crystallization (Comment) | Organism |
---|---|
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 | Comment | Organism |
---|---|---|
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 | Comment | Organism | Structure |
---|---|---|---|
4-carboxy-5-[(4-chlorophenyl)sulfanyl]-1,2,3-thiadiazole | CCPST | Rattus norvegicus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-lactate + O2 | Rattus norvegicus | - |
pyruvate + H2O2 | - |
? | |
an (S)-2-hydroxy carboxylate + O2 | Rattus norvegicus | - |
a 2-oxo carboxylate + H2O2 | - |
? | |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | Q07523 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
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 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-lactate + O2 | - |
Rattus norvegicus | pyruvate + H2O2 | - |
? | |
an (S)-2-hydroxy carboxylate + O2 | - |
Rattus norvegicus | a 2-oxo carboxylate + H2O2 | - |
? | |
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 | Comment | Organism |
---|---|---|
Hao2 | - |
Rattus norvegicus |
LCHAO | - |
Rattus norvegicus |
long-chain L-alpha-hydroxy acid oxidase | - |
Rattus norvegicus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FMN | dependent on | Rattus norvegicus |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the family of L-2-hydroxy acid oxidases | Rattus norvegicus |
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 |