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Information on EC 1.1.3.46 - 4-hydroxymandelate oxidase
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1.1.3.46 4-hydroxymandelate oxidaseIUBMB 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.
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Word Map
- 1.1.3.46
- oxidases
-
fmn-dependent
-
amycolatopsis
-
four-electron
- flavin
- coelicolor
- benzoylformate
-
two-electron
- mononucleotide
- vancomycin
-
nonribosomal
- orientalis
- chloroeremomycin
- synthesis
The enzyme appears in viruses and cellular organisms
Synonyms
hydroxymandelate oxidase, p-hydroxymandelate oxidase, 
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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
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-chloro-(S)-mandelate + O2
(2-chlorophenyl)(oxo)acetic acid + H2O2
-
-
-
?
4-bromo-(S)-mandelate + O2
(4-bromophenyl)(oxo)acetic acid + H2O2
-
-
-
?
4-chloro-(S)-mandelate + O2
(4-chlorophenyl)(oxo)acetic acid + H2O2
-
-
-
?
4-trifluoromethyl-(S)-mandelate + O2
(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
-
-
-
(S)-2-hydroxy-2-(4-hydroxyphenyl)acetate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
(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
2-(4-hydroxyphenyl)-2-oxoacetate i.e. 4-hydroxyphenylglyoxylate
-
?
(S)-2-hydroxy-2-(4-hydroxyphenyl)acetate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
(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
2-(4-hydroxyphenyl)-2-oxoacetate i.e. 4-hydroxyphenylglyoxylate
-
?
(S)-2-hydroxy-2-(4-hydroxyphenyl)acetate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
(S)-2-hydroxy-2-(4-hydroxyphenyl)acetate i.e. (S)-4-hydroxymandelate
2-(4-hydroxyphenyl)-2-oxoacetate i.e. 4-hydroxyphenylglyoxylate
-
?
(S)-3,5-dihydroxymandelate + O2
2-(3,5-dihydroxyphenyl)-2-oxoacetate + H2O2
-
-
-
?
(S)-3,5-dihydroxymandelate + O2
2-(3,5-dihydroxyphenyl)-2-oxoacetate + H2O2
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
-
-
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
-
-
-
-
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
-
-
-
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
-
-
-
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
-
-
-
-
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
-
-
-
-
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
-
-
-
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
-
-
-
-
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
-
-
-
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
-
-
-
?
(S)-mandelate + O2
2-phenyl-2-oxoacetate + H2O2
no activity with (R)-mandelate
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
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
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
-
-
?
(S)-2-hydroxy-2-(4-hydroxyphenyl)acetate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
(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
2-(4-hydroxyphenyl)-2-oxoacetate i.e. 4-hydroxyphenylglyoxylate
-
?
(S)-2-hydroxy-2-(4-hydroxyphenyl)acetate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
(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
2-(4-hydroxyphenyl)-2-oxoacetate i.e. 4-hydroxyphenylglyoxylate
-
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
-
-
-
-
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
-
-
-
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
-
-
-
-
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
-
-
-
-
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
-
-
-
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
-
-
-
-
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
-
-
-
?
(S)-4-hydroxymandelate + O2
2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
-
-
-
?
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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
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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
Streptomyces coelicolor, Amycolatopsis orientalis (O52791), Amycolatopsis orientalis
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, Streptomyces coelicolor, Streptomyces coelicolor CGMCC 4.1092, Amycolatopsis orientalis ATCC 19795
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
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Release 2023.1 (January 2023)
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