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Literature summary for 1.14.13.64 extracted from

  • Westphal, A.H.; Tischler, D.; van Berkel, W.J.H.
    Natural diversity of FAD-dependent 4-hydroxybenzoate hydroxylases (2021), Arch. Biochem. Biophys., 702, 108820 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene mnx1, sequence comparisons and phylogenetic analysis and tree, recombinant expression of C-terminally His-tagged enzyme in Escherichia coli strain TOP10 Candida parapsilosis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.01
-
4-hydroxybenzoate recombinant enzyme, pH 7.6, 25°C Candida parapsilosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-hydroxybenzoate + NADH + 2 H+ + O2 Candida parapsilosis
-
hydroquinone + NAD+ + H2O + CO2
-
?
4-hydroxybenzoate + NADH + 2 H+ + O2 Candida parapsilosis CBS604
-
hydroquinone + NAD+ + H2O + CO2
-
?

Organism

Organism UniProt Comment Textmining
Candida parapsilosis
-
-
-
Candida parapsilosis CBS604
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information 4HB1H does not contain a lipid cofactor Candida parapsilosis

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain TOP10 by nickel affinity chromatography, dialysis, ion exchange chromatography, and gel filtration Candida parapsilosis

Reaction

Reaction Comment Organism Reaction ID
4-hydroxybenzoate + NAD(P)H + H+ + O2 = hydroquinone + NAD(P)+ + H2O + CO2 the conversion of 4-HB involves an ipso-attack of the electrophilic flavin C4a-hydroperoxide at the C1-atom of the activated substrate, resulting in a tetrahedral benzoquinone species and subsequent release of the carboxyl side chain. It cannot be excluded that His230 activates 4-HB in 4HB1H for ipso-attack by the flavin C4a-hydroperoxide. Furthermore, it can also not be ruled out that the substrate of 4HB1H binds in a flipped orientation with the 4-hydroxyl moiety pointing towards the side chains of Tyr116 and His118 Candida parapsilosis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
14
-
purified recombinant enzyme, pH 7.6, 25°C, substrates 4-hydroxybenzoate and NADH Candida parapsilosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-hydroxybenzoate + NADH + 2 H+ + O2
-
Candida parapsilosis hydroquinone + NAD+ + H2O + CO2
-
?
4-hydroxybenzoate + NADH + 2 H+ + O2
-
Candida parapsilosis CBS604 hydroquinone + NAD+ + H2O + CO2
-
?
additional information 4HB1H catalyzes an oxidative decarboxylation reaction. 4HB1H is active with a wide range of 4-hydroxybenzoate (4-HB) derivatives. 4HB1H can also be induced by protocatechuate (PCA) and convert this compound directly into the central intermediate HHQ Candida parapsilosis ?
-
-
additional information 4HB1H catalyzes an oxidative decarboxylation reaction. 4HB1H is active with a wide range of 4-hydroxybenzoate (4-HB) derivatives. 4HB1H can also be induced by protocatechuate (PCA) and convert this compound directly into the central intermediate HHQ Candida parapsilosis CBS604 ?
-
-
protocatechuate + NADH + 2 H+ + O2
-
Candida parapsilosis hydroquinone + NAD+ + H2O + CO2
-
?
protocatechuate + NADH + 2 H+ + O2
-
Candida parapsilosis CBS604 hydroquinone + NAD+ + H2O + CO2
-
?
vanillate + NADH + 2 H+ + O2
-
Candida parapsilosis 3-methoxy-1,4-dihydroxybenzene + NAD+ + H2O + CO2
-
?
vanillate + NADH + 2 H+ + O2
-
Candida parapsilosis CBS604 3-methoxy-1,4-dihydroxybenzene + NAD+ + H2O + CO2
-
?

Subunits

Subunits Comment Organism
monomer
-
Candida parapsilosis

Synonyms

Synonyms Comment Organism
4-hydroxybenzoate 1-hydroxylase (decarboxylating)
-
Candida parapsilosis
4HB1H
-
Candida parapsilosis
Cp_4HB1H
-
Candida parapsilosis
FAD-dependent 4-hydroxybenzoate hydroxylase
-
Candida parapsilosis
PHBH
-
Candida parapsilosis
V1H
-
Candida parapsilosis
vanillate 1-hydroxylase
-
Candida parapsilosis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
-
Candida parapsilosis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
10
-
4-hydroxybenzoate recombinant enzyme, pH 7.6, 25°C Candida parapsilosis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
-
Candida parapsilosis

Cofactor

Cofactor Comment Organism Structure
FAD addition of FAD is essential to achieve optimal turnover Candida parapsilosis
additional information 4HB1H does not contain a lipid cofactor Candida parapsilosis
NADH highly preferred cofactor Candida parapsilosis

General Information

General Information Comment Organism
evolution phylogenetic analysis of FAD-dependent 4-hydroxybenzoate hydroxylases and 3-hydroxybenzoate 4-hydroxylase, phylogenetic analysis and tree, overview. Enzyme 4HB1H is only present in a small group of Saccharomycetes. Many FAD-binding proteins with unknown function in pezizomycetes and agaricomycetes have structural features in common with 4HB1H, but lack its C-terminal tail. 4HB1H belongs to a subgroup of structurally related group A FPMOs that catalyze para-hydroxylation reactions Candida parapsilosis
metabolism the enzyme is important in lignin degradation. The conversion of 4-hydroxybenzoate (4-HB) involves an ipso-attack of the electrophilic flavin C4a-hydroperoxide at the C1-atom of the activated substrate, resulting in a tetrahedral benzoquinone species and subsequent release of the carboxyl side chain. The second step of the catabolism of 4-HB in Candida parapsilosis catalyzed by the homodimeric hydroquinone hydroxylase, HQH Candida parapsilosis
additional information structure comparisons and protein homology modelling, generation of a model of Candida parapsilosis Cp_HQH and models for Cp_4HB1H, Fusarium oxysporum Fo_4HB1H-like, and Boreostereum vibrans Bv_VibMO1 using Cutaneotrichosporon cutaneum Tc_PHHY (PDB ID 1pn0), Rhodococcus jostii Rj_3HB6H (PDB ID 4bk1) and Pseudomonas putida Pp_SALH (PDB ID 5evy) as template structures, overview Candida parapsilosis
physiological function 4-hydroxybenzoate 1-hydroxylase (4HB1H) from yeast catalyzes an oxidative decarboxylation reaction and is structurally similar to 3-hydroxybenzoate 6-hydroxylase (3HB6H), salicylate hydroxylase (SALH) and 6-hydroxynicotinate 3-monooxygenase (6HNMO). Genome mining suggests that the 4HB1H activity is widespread in the fungal kingdom and might be responsible for the oxidative decarboxylation of vanillate, an import intermediate in lignin degradation Candida parapsilosis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1000
-
4-hydroxybenzoate recombinant enzyme, pH 7.6, 25°C Candida parapsilosis