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Information on EC 1.13.11.15 - 3,4-dihydroxyphenylacetate 2,3-dioxygenase

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IUBMB Comments
An iron protein.
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This record set is specific for:
UNIPROT: Q45135
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
homoprotocatechuate 2,3-dioxygenase, 3,4-dihydroxyphenylacetate 2,3-dioxygenase, fehpcd, padhpao, 2,3-hpcd, fe-hpcd, mn-hpcd, dhpao, hpado, mnhpcd, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homoprotocatechuate 2,3-dioxygenase
homoprotocatechuate dioxygenase
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HPCA 2,3-dioxygenase
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3,4-dihydroxyphenylacetic acid 2,3-dioxygenase
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homoprotocatechuate 2,3-dioxygenase
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HPADO
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HPC dioxygenase
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HPCD
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oxygenase, homoprotocatechuate 2,3-di-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
3,4-dihydroxyphenylacetate:oxygen 2,3-oxidoreductase (decyclizing)
An iron protein.
CAS REGISTRY NUMBER
COMMENTARY hide
37256-56-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3,4-dihydroxyphenylacetate + O2
1-carboxymethyl-4-hydroxy-cis-muconic semialdehyde
show the reaction diagram
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-
-
?
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
show the reaction diagram
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-
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?
4-nitrocatechol + O2
(2Z,4Z)-2-hydroxy-4-nitro-6-oxohexa-2,4-dienoate
show the reaction diagram
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-
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?
4-nitrocatechol + O2
(2Z,4Z)-2-hydroxy-5-nitro-6-oxohexa-2,4-dienoate
show the reaction diagram
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?
4-nitrocatechol + O2
?
show the reaction diagram
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3,4-dihydroxyphenylacetate + O2
2-hydroxy-5-carboxymethylmuconate semialdehyde
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the catalytic reaction with substrate 4-nitrocatechol is comprised of four steps: (1) A dioxygen attacks the aromatic ring to produce an alkylperoxo species. (2) O-O bond cleavage and the formation of an epoxide species occur. (3) A seven-membered O-heterocyclic compound is generated by the extinction of the epoxy structure. (4) The seven-membered ring undergoes ring opening to form the final product (C2-C3 cleavage product). The effective free energy barrier of the catalytic reaction of the system is 26.2 kcal/mol
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q45135_9MICO
365
0
41699
TrEMBL
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallizations of wild-type FeHPCD and mutant Y257F with bound substrates 3,4-dihydroxyphenylacetate and 4-nitrocatechol, hanging drop vapour diffusion method, in either 13% PEG 6000, 0.1 M calcium chloride, 0.1 M Tris-HCl, pH 6.5-7.4 or in 18% PEG 8000, 0.1 M calcium acetate, 0.1 M sodium cacodylate, pH 6.5, at 20°C, cryoprotectant solution containing either 20-25% PEG400 or 20% glycerol in the mother liquor solution, X-ray diffraction structure determination and analysis at 1.50-1.60 A resolution
molecular docking of metsulfuron-methyl and chlorsulfon
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H200N
variant employs a C4 (para-carbon) pathway to produce a C4-C5 cleavage product
Y257F
site-directed mutagenesis, changes in kinetics for Y257F variant can be attributed to the loss of interactions between substrate and Tyr257, substrate binding structures compared to the wild-type enzyme, overview
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
degradation
comparison of binding sites and affinities using substrates chlorsulfon and metsulfuron-methyl. Homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum and Arthrobacter globiformis are more effective in binding than catechol 2,3-dioxygenase from Pseudomonas putida. B. fuscum and A. globiformis have more potential than P. putida to remediate chlorsulfuron and metsulfuronmethyl
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Xu, L.; Zhao, W.; Wang, X.
Finding molecular dioxygen tunnels in homoprotocatechuate 2,3-dioxygenase: implications for different reactivity of identical subunits
Eur. Biophys. J.
39
327-336
2009
Brevibacterium fuscum (Q45135)
Manually annotated by BRENDA team
Georgiev, V.; Borowski, T.; Blomberg, M.R.; Siegbahn, P.E.
A comparison of the reaction mechanisms of iron- and manganese-containing 2,3-HPCD: an important spin transition for manganese
J. Biol. Inorg. Chem.
13
929-940
2008
Brevibacterium fuscum (Q45135), Brevibacterium fuscum
Manually annotated by BRENDA team
Xu, L.; Liu, X.; Zhao, W.; Wang, X.
Locally enhanced sampling study of dioxygen diffusion pathways in homoprotocatechuate 2,3-dioxygenase
J. Phys. Chem. B
113
13596-13603
2009
Brevibacterium fuscum (Q45135)
Manually annotated by BRENDA team
Kovaleva, E.G.; Lipscomb, J.D.
Structural basis for the role of tyrosine 257 of homoprotocatechuate 2,3-dioxygenase in substrate and oxygen activation
Biochemistry
51
8755-8763
2012
Brevibacterium fuscum (Q45135)
Manually annotated by BRENDA team
Bauri, S.; Sen, M.; Das, R.; Mondal, S.
In-silico investigation of the efficiency of microbial dioxygenases in degradation of sulfonylurea group herbicides
Bioremediat. J.
26
76-87
2022
Arthrobacter globiformis (Q44048), Brevibacterium fuscum (Q45135)
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Manually annotated by BRENDA team
Tu, N.; Zhang, D.; Niu, X.; Du, C.; Zhang, L.; Xie, W.; Niu, X.; Liu, Y.; Li, Y.
A novel concept for the biodegradation mechanism of dianionic catechol with homoprotocatechuate 2,3-dioxygenase A non-proton-assisted process
Chemosphere
246
125796
2020
Brevibacterium fuscum (Q45135)
Manually annotated by BRENDA team