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Information on EC 1.1.3.46 - 4-hydroxymandelate oxidase
for references in articles please use BRENDA:EC1.1.3.46
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.3 With oxygen as acceptor
1.1.3.46 4-hydroxymandelate oxidase
IUBMB Comments
A flavoprotein (FMN). The enzyme from the bacterium Amycolatopsis orientalis is involved in the biosynthesis of L-(4-hydroxyphenyl)glycine and L-(3,5-dihydroxyphenyl)glycine, two non-proteinogenic amino acids occurring in the vancomycin group of antibiotics.
The enzyme appears in viruses and cellular organisms
- 1.1.3.46
- oxidases
-
fmn-dependent
-
amycolatopsis
-
four-electron
- flavin
- coelicolor
- benzoylformate
-
two-electron
- mononucleotide
- vancomycin
-
nonribosomal
- orientalis
- chloroeremomycin
- synthesis
showSynonyms
hydroxymandelate oxidase, p-hydroxymandelate oxidase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
fegC
HmO
hydroxymandelate oxidase
L-4-hydroxymandelate oxidase
p-hydroxymandelate oxidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-4-hydroxymandelate + O2 = 2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
(S)-4-hydroxymandelate:oxygen 1-oxidoreductase
A flavoprotein (FMN). The enzyme from the bacterium Amycolatopsis orientalis is involved in the biosynthesis of L-(4-hydroxyphenyl)glycine and L-(3,5-dihydroxyphenyl)glycine, two non-proteinogenic amino acids occurring in the vancomycin group of antibiotics.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-3-phenyllactate + O2
phenylpyruvate + H2O2
Substrates: -
Products: -
Products: -
?
(S)-mandelate + O2
2-phenyl-2-oxoacetate
Substrates: -
Products: -
Products: -
?
2 (S)-mandelate + O2
2 benzoate + 2 CO2
Substrates: -
Products: -
Products: -
?
2-chloro-(S)-mandelate + O2
(2-chlorophenyl)(oxo)acetic acid + H2O2
Substrates: -
Products: -
Products: -
?
4-bromo-(S)-mandelate + O2
(4-bromophenyl)(oxo)acetic acid + H2O2
Substrates: -
Products: -
Products: -
?
4-chloro-(S)-mandelate + O2
(4-chlorophenyl)(oxo)acetic acid + H2O2
Substrates: -
Products: -
Products: -
?
4-trifluoromethyl-(S)-mandelate + O2
(4-trifluoromethylphenyl)(oxo)acetic acid + H2O2
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: O2 is the prerequisite electron acceptor in the oxidation reaction. No substrates: (R)-4-hydroxymandelate, (S)-2-methylphenylacetate
Products: -
Products: -
-
(S)-2-hydroxy-2-(4-hydroxyphenyl)acetate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
Substrates: (S)-2-hydroxy-2-(4-hydroxyphenyl)acetate i.e. (S)-4-hydroxymandelate. The enzyme is involed in the biosynthesis of (S)-4-hydroxyphenylglycine and (S)-3,5-dihydroxyphenylglycine, two non-proteinogenic amino acids occurring in the vancomycin group of antibiotics
Products: 2-(4-hydroxyphenyl)-2-oxoacetate i.e. 4-hydroxyphenylglyoxylate
Products: 2-(4-hydroxyphenyl)-2-oxoacetate i.e. 4-hydroxyphenylglyoxylate
?
(S)-2-hydroxy-2-(4-hydroxyphenyl)acetate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
Substrates: (S)-2-hydroxy-2-(4-hydroxyphenyl)acetate i.e. (S)-4-hydroxymandelate. The enzyme is involed in the biosynthesis of the non-proteinogenic amino acid (S)-4-hydroxyphenylglycine a constituent of peptide antibiotics
Products: 2-(4-hydroxyphenyl)-2-oxoacetate i.e. 4-hydroxyphenylglyoxylate
Products: 2-(4-hydroxyphenyl)-2-oxoacetate i.e. 4-hydroxyphenylglyoxylate
?
(S)-2-hydroxy-2-(4-hydroxyphenyl)acetate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
Substrates: (S)-2-hydroxy-2-(4-hydroxyphenyl)acetate i.e. (S)-4-hydroxymandelate
Products: 2-(4-hydroxyphenyl)-2-oxoacetate i.e. 4-hydroxyphenylglyoxylate
Products: 2-(4-hydroxyphenyl)-2-oxoacetate i.e. 4-hydroxyphenylglyoxylate
?
(S)-3,5-dihydroxymandelate + O2
2-(3,5-dihydroxyphenyl)-2-oxoacetate + H2O2
Substrates: -
Products: -
Products: -
?
(S)-3,5-dihydroxymandelate + O2
2-(3,5-dihydroxyphenyl)-2-oxoacetate + H2O2
Substrates: the enzyme is involed in the biosynthesis of (S)-4-hydroxyphenylglycine and (S)-3,5-dihydroxyphenylglycine, two non-proteinogenic amino acids occurring in the vancomycin group of antibiotics
Products: -
Products: -
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
-
Substrates: -
Products: -
Products: -
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
Substrates: -
Products: -
Products: -
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
Substrates: -
Products: -
Products: -
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
-
Substrates: -
Products: -
Products: -
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
-
Substrates: -
Products: -
Products: -
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
Substrates: -
Products: -
Products: -
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
-
Substrates: -
Products: -
Products: -
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
Substrates: -
Products: -
Products: -
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
Substrates: -
Products: -
Products: -
?
(S)-mandelate + O2
2-phenyl-2-oxoacetate + H2O2
Substrates: -
Products: -
Products: -
?
(S)-mandelate + O2
2-phenyl-2-oxoacetate + H2O2
Substrates: no activity with (R)-mandelate
Products: -
Products: -
?
4-hydroxyphenylpyruvate + O2
phenylpyruvate + H2O2
Substrates: -
Products: -
Products: -
?
4-hydroxyphenylpyruvate + O2
phenylpyruvate + H2O2
-
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-3,5-dihydroxymandelate + O2
2-(3,5-dihydroxyphenyl)-2-oxoacetate + H2O2
Substrates: the enzyme is involed in the biosynthesis of (S)-4-hydroxyphenylglycine and (S)-3,5-dihydroxyphenylglycine, two non-proteinogenic amino acids occurring in the vancomycin group of antibiotics
Products: -
Products: -
?
(S)-2-hydroxy-2-(4-hydroxyphenyl)acetate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
Substrates: (S)-2-hydroxy-2-(4-hydroxyphenyl)acetate i.e. (S)-4-hydroxymandelate. The enzyme is involed in the biosynthesis of (S)-4-hydroxyphenylglycine and (S)-3,5-dihydroxyphenylglycine, two non-proteinogenic amino acids occurring in the vancomycin group of antibiotics
Products: 2-(4-hydroxyphenyl)-2-oxoacetate i.e. 4-hydroxyphenylglyoxylate
Products: 2-(4-hydroxyphenyl)-2-oxoacetate i.e. 4-hydroxyphenylglyoxylate
?
(S)-2-hydroxy-2-(4-hydroxyphenyl)acetate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
Substrates: (S)-2-hydroxy-2-(4-hydroxyphenyl)acetate i.e. (S)-4-hydroxymandelate. The enzyme is involed in the biosynthesis of the non-proteinogenic amino acid (S)-4-hydroxyphenylglycine a constituent of peptide antibiotics
Products: 2-(4-hydroxyphenyl)-2-oxoacetate i.e. 4-hydroxyphenylglyoxylate
Products: 2-(4-hydroxyphenyl)-2-oxoacetate i.e. 4-hydroxyphenylglyoxylate
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
-
Substrates: -
Products: -
Products: -
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
Substrates: -
Products: -
Products: -
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
-
Substrates: -
Products: -
Products: -
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
-
Substrates: -
Products: -
Products: -
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
Substrates: -
Products: -
Products: -
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
-
Substrates: -
Products: -
Products: -
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
Substrates: -
Products: -
Products: -
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the enzyme is involed in the biosynthesis of L-(4-hydroxyphenyl)glycine and L-(3,5-dihydroxyphenyl)glycine, two non-proteinogenic amino acids occurring in the vancomycin group of antibiotics
Show AA Sequence and Transmembrane Helices (137 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structures of Hmo and its mutants in complex with physiological/nonphysiological substrates, products and inhibitors
structures of wild-type and mutant Y128F with and without substrate. Cofactor FMNox possesses an electrophilic/nucleophilic duality. In the Y128F mutant the active-site perturbation ensemble facilitates the polarization of FMNox to a nucleophilic ylide, which is in a position to act on an alpha-ketoacid, forming an N5-acyl-FMNred dead-end adduct. In four-electron oxidation of mutant Y128F, an intramolecular disproportionation reaction via an N5-alkanol-FMNred C'alpha carbanion intermediate may account for the ThDP/PLP/NADPH-independent oxidative decarboxylation reaction
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Y128F
Y128F
mutant extends the two-electron oxidation reaction to a four-electron oxidative decarboxylation reaction
Y128F
mutant is capable of oxidizing mandelate to benzoate via a four-electron oxidative decarboxylation reaction
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap affinity column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Top10 cells
expression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
whole-cell bioconversion of L-tyrosine into protocatechuic acid using artificial enzymatic cascades engineered in Escherichia coli. The first biocatalytic route comprises L-amino acid deaminase (LAAD) from Proteus mirabilis, hydroxymandelate synthase (HmaS) from Amycolatopsis orientalis, two-component flavin-dependent monooxygenase (HpaBC) from Escherichia coli, hydroxymandelate oxidase (HMO) from Streptomyces coelicolor, benzoylformate decarboxylase (BFD) from Pseudomonas putida, and aldehyde dehydrogenase (ALDH) from Saccharomyces cerevisiae. Combining LAAD/HmaS/HpaBC results in efficient synthesis of 3,4-dihydroxymandelate, which can be further converted to protocatechuic acid by HMO/BFD/ALDH to a final conversion of 64.4%. The recombinant E. coli catalyzes >99% conversion of L-tyrosine into 4-hydroxybenzoate within 12 h, further incorporation of 4-hydroxybenzoate hydroxylase PobA results in complete conversion of 4-hydroxybenzoate into protocatechuic acid, reaching >99% conversion
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mller, U.; van Assema, F.; Gunsior, M.; Orf, S.; Kremer, S.; Schipper, D.; Wagemans, A.; Townsend, C.A.; Sonke, T.; Bovenberg, R.; Wubbolts, M.
Metabolic engineering of the E. coli L-phenylalanine pathway for the production of D-phenylglycine (D-Phg)
Metab. Eng.
8
196-208
2006
Amycolatopsis orientalis (O52791), Amycolatopsis orientalis, Streptomyces coelicolor
brenda
Hubbard, B.K.; Thomas, M.G.; Walsh, C.T.
Biosynthesis of L-p-hydroxyphenylglycine, a non-proteinogenic amino acid constituent of peptide antibiotics
Chem. Biol.
7
931-942
2000
Amycolatopsis orientalis (G4V4S8), Amycolatopsis orientalis
brenda
Li, T.L.; Choroba, O.W.; Charles, E.H.; Sandercock, A.M.; Williams, D.H.; Spencer, J.B.
Characterisation of a hydroxymandelate oxidase involved in the biosynthesis of two unusual amino acids occurring in the vancomycin group of antibiotics
Chem. Commun. (Camb. )
21
1752-1753
2001
Amycolatopsis orientalis (G4V4S8)
brenda
Liu, S.P.; Liu, R.X.; El-Rotail, A.A.; Ding, Z.Y.; Gu, Z.H.; Zhang, L.; Shi, G.Y.
Heterologous pathway for the production of L-phenylglycine from glucose by E. coli
J. Biotechnol.
186C
91-97
2014
Amycolatopsis orientalis, Amycolatopsis orientalis ATCC 19795, Streptomyces coelicolor, Streptomyces coelicolor CGMCC 4.1092
brenda
Diez, V.; Loznik, M.; Taylor, S.; Winn, M.; Rattray, N.J.; Podmore, H.; Micklefield, J.; Goodacre, R.; Medema, M.H.; Mueller, U.; Bovenberg, R.; Janssen, D.B.; Takano, E.
Functional exchangeability of oxidase and dehydrogenase reactions in the biosynthesis of hydroxyphenylglycine, a nonribosomal peptide building block
ACS Synth. Biol.
4
796-807
2015
Streptomyces coelicolor (Q9Z4X8), Streptomyces coelicolor
brenda
Gonsior, M.; Muehlenweg, A.; Tietzmann, M.; Rausch, S.; Poch, A.; Suessmuth, R.D.
Biosynthesis of the peptide antibiotic feglymycin by a linear nonribosomal peptide synthetase mechanism
ChemBioChem
16
2610-2614
2015
Streptomyces sp. (A0A0P0KG57), Streptomyces sp. DSM11171 (A0A0P0KG57)
brenda
Chen, Y.; Wu, P.; Ko, L.; Kao, T.; Liu, L.; Zhang, Y.; Yuan, J.
High-yielding protocatechuic acid synthesis from l -tyrosine in Escherichia coli
ACS Sust. Chem. Eng.
8
14949-14954
2020
Streptomyces coelicolor
-
brenda
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
Acta Crystallogr. Sect. D
75
733-742
2019
Amycolatopsis orientalis (O52792)
brenda
Lyu, S.; Lin, K.; Yeh, H.; Li, Y.; Huang, C.; Wang, Y.; Shih, H.; Hsu, N.; Wu, C.; Li, T.
The flavin mononucleotide cofactor in alpha-hydroxyacid oxidases exerts its electrophilic/nucleophilic duality in control of the substrate-oxidation level
Acta Crystallogr. Sect. D
75
918-929
2019
Amycolatopsis orientalis (O52792)
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.3.46)
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