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Literature summary for 1.1.3.46 extracted from

  • Yeh, H.; Lin, K.; Lyu, S.; Li, Y.; Huang, C.; Wang, Y.; Shih, H.; Hsu, N.; Wu, C.; Li, T.
    Biochemical and structural explorations of a-hydroxyacid oxidases reveal a four-electron oxidative decarboxylation reaction (2019), Acta Crystallogr. Sect. D, 75, 733-742 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.3.46

Crystallization (Commentary)

Crystallization (Comment) Organism
structures of Hmo and its mutants in complex with physiological/nonphysiological substrates, products and inhibitors Amycolatopsis orientalis

Protein Variants

Protein Variants Comment Organism
H252F no catalytic activity Amycolatopsis orientalis
Y128F mutant extends the two-electron oxidation reaction to a four-electron oxidative decarboxylation reaction Amycolatopsis orientalis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.13
-
 (S)-Mandelate mutant Y128F, pH 7,5, 25°C Amycolatopsis orientalis
0.16
-
 (S)-Mandelate pH 7,5, 25°C Amycolatopsis orientalis

Organism

Organism UniProt Comment Textmining
Amycolatopsis orientalis O52792
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-3-phenyllactate + O2
-
 Amycolatopsis orientalis phenylpyruvate + H2O2
-
 ?
(S)-4-hydroxymandelate + O2
-
 Amycolatopsis orientalis 2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
-
 ?
(S)-mandelate + O2
-
 Amycolatopsis orientalis 2-phenyl-2-oxoacetate
-
 ?
2-chloro-(S)-mandelate + O2
-
 Amycolatopsis orientalis (2-chlorophenyl)(oxo)acetic acid + H2O2
-
 ?
4-bromo-(S)-mandelate + O2
-
 Amycolatopsis orientalis (4-bromophenyl)(oxo)acetic acid + H2O2
-
 ?
4-chloro-(S)-mandelate + O2
-
 Amycolatopsis orientalis (4-chlorophenyl)(oxo)acetic acid + H2O2
-
 ?
4-trifluoromethyl-(S)-mandelate + O2
-
 Amycolatopsis orientalis (4-trifluoromethylphenyl)(oxo)acetic acid + H2O2
-
 ?
additional information O2 is the prerequisite electron acceptor in the oxidation reaction. No substrates: (R)-4-hydroxymandelate, (S)-2-methylphenylacetate Amycolatopsis orientalis ?
-
-

Synonyms

Synonyms Comment Organism
HmO
-
 Amycolatopsis orientalis
p-hydroxymandelate oxidase
-
 Amycolatopsis orientalis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.05
-
 (S)-Mandelate mutant Y128F, pH 7,5, 25°C Amycolatopsis orientalis
5.17
-
 (S)-Mandelate wild-type, pH 7,5, 25°C Amycolatopsis orientalis

Cofactor

Cofactor Comment Organism Structure
FMN in the two-electron oxidation reaction, FMNox is reduced by a hydride directly from an alpha-hydroxyacid. FMNred is instantly oxidized by O2 to yield H2O2 Amycolatopsis orientalis