KEGG   ENZYME: 1.17.9.1Help
Entry
EC 1.17.9.1                 Enzyme                                 

Name
4-methylphenol dehydrogenase (hydroxylating);
pchCF (gene names);
p-cresol-(acceptor) oxidoreductase (hydroxylating);
p-cresol methylhydroxylase;
4-cresol dehydrogenase (hydroxylating)
Class
Oxidoreductases;
Acting on CH or CH2 groups
BRITE hierarchy
Sysname
4-methylphenol:oxidized azurin oxidoreductase (methyl-hydroxylating)
Reaction(IUBMB)
4-methylphenol + 4 oxidized azurin + H2O = 4-hydroxybenzaldehyde + 4 reduced azurin + 4 H+ (overall reaction) [RN:R02675];
(1a) 4-methylphenol + 2 oxidized azurin + H2O = 4-hydroxybenzyl alcohol + 2 reduced azurin + 2 H+ [RN:R12133];
(1b) 4-hydroxybenzyl alcohol + 2 oxidized azurin = 4-hydroxybenzaldehyde + 2 reduced azurin + 2 H+ [RN:R12134]
Reaction(KEGG)
Substrate
4-methylphenol [CPD:C01468];
oxidized azurin [CPD:C05357];
H2O [CPD:C00001];
4-hydroxybenzyl alcohol [CPD:C17467]
Product
4-hydroxybenzaldehyde [CPD:C00633];
reduced azurin [CPD:C05358];
H+ [CPD:C00080];
4-hydroxybenzyl alcohol [CPD:C17467]
Comment
This bacterial enzyme contains a flavin (FAD) subunit and a cytochrome c subunit. The flavin subunit abstracts two hydrogen atoms from the substrate, forming a quinone methide intermediate, then hydrates the latter at the benzylic carbon with a hydroxyl group derived from water. The protons are lost to the bulk solvent, while the electrons are passed to the heme on the cytochrome subunit, and from there to azurin, a small copper-binding protein that is co-localized with the enzyme in the periplasm. The first hydroxylation forms 4-hydroxybenzyl alcohol; a second hydroxylation converts this into 4-hydroxybenzaldehyde.
History
EC 1.17.9.1 created 1983 as EC 1.17.99.1, modified 2001, modified 2011, modified 2015, transferred 2018 to EC 1.17.9.1
Pathway
ec00623  Toluene degradation
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
K05797  4-cresol dehydrogenase (hydroxylating) flavoprotein subunit
Genes
SERM: CLM71_00285
BRB: EH207_06030 EH207_06350
XHY: FZ025_04795
RBD: ALSL_0887 ALSL_0892
VCY: IX92_07590
VCT: JV59_30920
PCQ: PcP3B5_13510(pchF_1) PcP3B5_26440(pchF_2) PcP3B5_26540(pchF_3)
PPUT: L483_22020
PDR: H681_14085
PALK: PSAKL28_20190 PSAKL28_30910 PSAKL28_31390
PSOS: POS17_3788(Neut_0635) POS17_5141(pchF)
PSET: THL1_645
PSIL: PMA3_18570
SWP: swp_2498
PAT: Patl_1202
AMAL: I607_13235
AMAE: I876_13620
AMAO: I634_13480
AMAD: I636_13600
AMAI: I635_13970
AMAC: MASE_13080
AAUS: EP12_13795
GNI: GNIT_2517
CJA: CJA_1090
MMAI: sS8_0581
NOC: Noc_2406
NHL: Nhal_1759
NWA: Nwat_1784
OCE: GU3_14310
BYI: BYI23_B003260(pchF)
BUE: BRPE67_BCDS05760(pchF)
BXE: Bxe_A2781
BXB: DR64_464(pchF)
BPH: Bphy_1706
BFN: OI25_3960(pchF)
AFQ: AFA_05565
PNA: Pnap_3838
VEI: Veis_0959
NEU: NE0741
EBA: ebA300(pchF) ebA310 ebA3165(pchF) ebA5380
AZA: AZKH_2917
CCOF: VC76_00030(pchF_2)
CCOO: ATE51_00010(pchF)
CURE: CUREO_0963
SULJ: SJPD1_1025
GME: Gmet_2125(pcmI)
GEO: Geob_0119(pcmI)
GEM: GM21_2847
CCX: COCOR_00350(pchF)
SPHR: BSY17_949
AAY: WYH_02883(pchF_1) WYH_03108(pchF_2) WYH_03116(pchF_3) WYH_03119(pchF_4)
RRU: Rru_A3112
RRF: F11_15945
MAGQ: MGMAQ_0999
GOM: D7316_03404(pchF)
SALS: SLNWT_0108
SRN: A4G23_02275(pchF)
STRD: NI25_07845
SMAL: SMALA_8211
MLV: CVS47_02783(pchF)
NDA: Ndas_1184
MMAR: MODMU_2955(vaoA)
ACTN: L083_7156
MPK: VL20_5235
TTF: THTE_3672
SUS: Acid_2038
CBAT: M666_16590
NDE: NIDE0022(pchF)
 » show all
Taxonomy
Reference
1  [PMID:588247]
  Authors
Hopper DJ, Taylor DG.
  Title
The purification and properties of p-cresol-(acceptor) oxidoreductase (hydroxylating), a flavocytochrome from Pseudomonas putida.
  Journal
Biochem J 167:155-62 (1977)
DOI:10.1042/bj1670155
Reference
2  [PMID:7391034]
  Authors
McIntire W, Edmondson DE, Singer TP, Hopper DJ.
  Title
8 alpha-O-Tyrosyl-FAD: a new form of covalently bound flavin from p-cresol methylhydroxylase.
  Journal
J Biol Chem 255:6553-5 (1980)
Reference
3  [PMID:3920077]
  Authors
Hopper DJ, Jones MR, Causer MJ
  Title
Periplasmic location of p-cresol methylhydroxylase in Pseudomonas putida.
  Journal
FEBS Lett 182:485-8 (1985)
DOI:10.1016/0014-5793(85)80359-8
Reference
4  [PMID:2722739]
  Authors
Bossert ID, Whited G, Gibson DT, Young LY.
  Title
Anaerobic oxidation of p-cresol mediated by a partially purified methylhydroxylase from a denitrifying bacterium.
  Journal
J Bacteriol 171:2956-62 (1989)
DOI:10.1128/JB.171.6.2956-2962.1989
Reference
5  [PMID:1697166]
  Authors
Reeve CD, Carver MA, Hopper DJ
  Title
Stereochemical aspects of the oxidation of 4-ethylphenol by the bacterial enzyme  4-ethylphenol methylenehydroxylase.
  Journal
Biochem J 269:815-9 (1990)
DOI:10.1042/bj2690815
Reference
6  [PMID:17449613]
  Authors
Peters F, Heintz D, Johannes J, van Dorsselaer A, Boll M
  Title
Genes, enzymes, and regulation of para-cresol metabolism in Geobacter metallireducens.
  Journal
J Bacteriol 189:4729-38 (2007)
DOI:10.1128/JB.00260-07
Reference
7  [PMID:18658262]
  Authors
Johannes J, Bluschke A, Jehmlich N, von Bergen M, Boll M
  Title
Purification and characterization of active-site components of the putative p-cresol methylhydroxylase membrane complex from Geobacter metallireducens.
  Journal
J Bacteriol 190:6493-500 (2008)
DOI:10.1128/JB.00790-08
Other DBs
ExplorEnz - The Enzyme Database: 1.17.9.1
IUBMB Enzyme Nomenclature: 1.17.9.1
ExPASy - ENZYME nomenclature database: 1.17.9.1
BRENDA, the Enzyme Database: 1.17.9.1
CAS: 66772-07-4

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