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Overview for MACiE Entry M0131

Version history

General Information

EC Number: 1.14.13.2 (A member of the Oxidoreductases, Acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2, With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor)

Enzyme Name: 4-hydroxybenzoate 3-monooxygenase

Biological Species: Pseudomonas aeruginosa (Bacteria)

Catalytic Chain UniprotKB Accession Codes:

  • P20586 - P-hydroxybenzoate hydroxylase

Representative PDB Code: 1doc - THE MOBIL FLAVIN OF 4-OH BENZOATE HYDROXYLASE: MOTION OF A PROSTHETIC GROUP REGULATES CATALYSIS (Resolution = 2.00 Å).

Catalytic CATH Codes:

Display structure information

Overall Reaction:

Image of NADPH

Image of oxygen

Image of 4-hydroxybenzoate

right arrow

Image of NADP

Image of water

Image of 3,4-dihydroxybenzoate

NADPH
C00005
CHEBI:16474
oxygen
C00007
CHEBI:15379
4-hydroxybenzoate
C00156
CHEBI:17879
NADP
C00006
CHEBI:18009
water
C00001
CHEBI:15377
3,4-dihydroxybenzoate
C00230
CHEBI:36241

View similar reactions


Stepwise Description of the Reaction

Step 1In a proton transfer chain involving His72-water-water-Tyr385-Tyr201 water deprotonates the 4-hydroxybenzoate substrate.
Step 2A conformational change allows NADP to bind, which initiates a reverse of the first proton transfer and a hydride transfer from NADP to the FAD cofactor.
Step 3FAD undergoes a double bond rearrangement that results in the single electron transfer from FAD to dioxygen.
Step 4The FAD and dioxygen radical species undergo a colligation reaction to form the FAD-peroxo adduct.
Step 5The FAD-peroxo adduct deprotonates a water molecule.
Step 6In a proton transfer chain involving His72-water-water-Tyr385-Tyr201 water deprotonates the 4-hydroxybenzoate substrate. The substrate undergoes a double bond rearrangement that results in the ortho-position attacking the FAD-peroxo adduct in a nucleophilic substitution that cleaves the O-O bond.
Step 7The FAD intermediate deprotonates the hydorxylated aromatic intermediate, cleaving the C-H bond and initiating a double bond rearrangement to yield 3,4-dihydroxybenzoic acid. This then takes a proton from water through the His72-water-water-Tyr385-Tyr201 proton transfer chain.
Step 8Water deprotonates the 3,4-dihydroxybenzoic acid through the His72-water-water-Tyr385-Tyr201 proton transfer chain.
Step 9The FAD-bound hydroxyl group initiates an intramolecular elimination of water, regenerating the FAD cofactor.

View similar reactions (composite manual annotation)


Catalytic Residues Involved

Type Number Chain Location of Function
His 72 A Side Chain
Tyr 201 A Side Chain
Pro 293 A Main Chain Carbonyl
Lys 297 A Side Chain
Tyr 385 A Side Chain

Organic Cofactors for M0131

Type Identity Chain
FAD FAD 395 Overview

References

  1. B. Entsch et al. (2005), Arch. Biochem. Biophys., 433, 297-311. Protein dynamics and electrostatics in the function of p-hydroxybenzoate hydroxylase.
    Medline: 15581585
  2. M. Ortiz-Maldonado et al. (2004), Biochemistry, 43, 15246-15257. Oxygen reactions in p-hydroxybenzoate hydroxylase utilize the H-bond network during catalysis.
    Medline: 15568817

Homologue information for M0131 (1doc)

CSA Homologues

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)



Entries with at least one Catalytic CATH code in common (different mechanisms):

MACiE Entry Enzyme Name
EC Number
PDB code CATH code Composite
Reaction Similarity
Catalytic Machinery
Similarity
M0294 succinate dehydrogenase (ubiquinone)
1.3.5.1
1yq4 3.50.50.60
0.0530.1058Compare
M0020 succinate dehydrogenase
1.3.99.1
1qjd 3.50.50.60
0.15480.0946Compare
M0113 sarcosine oxidase
1.5.3.1
2gb0 3.50.50.60
3.30.9.10
0.25120.2583Compare
M0006 glutathione-disulfide reductase
1.8.1.7
2gh5 3.50.50.60
0.05490.1199Compare
M0123 adenylyl-sulfate reductase
1.8.99.2
1jnr 3.50.50.60
0.0880.0630Compare
M0142 ferredoxin-NADP+ reductase
1.18.1.2
1e6e 3.50.50.60
0.03960.1038Compare

View a comparison of the other reactions in MACiE with the CATH domain 3.30.9.10

View a comparison of the other reactions in MACiE with the CATH domain 3.50.50.60


Links to this entry in other databases

Link to EC-PDB-SUM Link to PDB-SUM Link to RCSB PDB Link to PDBe Link to CSA
Link to MetaCyc Link to KEGG Link to BRENDA Link to ExplorENZ
Link to EzCatDB

GOA logo
monooxygenase activity (molecular function)
metabolic process (biological process)
oxidoreductase activity (molecular function)
4-hydroxybenzoate 3-monooxygenase activity (molecular function)
aromatic compound catabolic process (biological process)
benzoate catabolic process (biological process)
flavin adenine dinucleotide binding (molecular function)
oxidation-reduction process (biological process)
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