KEGG   ENZYME: 1.3.99.8Help
Entry
EC 1.3.99.8                 Enzyme                                 

Name
2-furoyl-CoA dehydrogenase;
furoyl-CoA hydroxylase;
2-furoyl coenzyme A hydroxylase;
2-furoyl coenzyme A dehydrogenase;
2-furoyl-CoA:(acceptor) 5-oxidoreductase (hydroxylating)
Class
Oxidoreductases;
Acting on the CH-CH group of donors;
With unknown physiological acceptors
BRITE hierarchy
Sysname
2-furoyl-CoA:acceptor 5-oxidoreductase (hydroxylating)
Reaction(IUBMB)
2-furoyl-CoA + H2O + acceptor = S-(5-hydroxy-2-furoyl)-CoA + reduced acceptor [RN:R02987]
Reaction(KEGG)
Substrate
2-furoyl-CoA [CPD:C00845];
H2O [CPD:C00001];
acceptor [CPD:C00028]
Product
S-(5-hydroxy-2-furoyl)-CoA [CPD:C03724];
reduced acceptor [CPD:C00030]
Comment
A copper protein. The oxygen atom of the -OH produced is derived from water, not O2; the actual oxidative step is probably dehydrogenation of a hydrated form -CHOH-CH2- to -C(OH)=CH-, which tautomerizes non-enzymically to -CO-CH2-, giving (5-oxo-4,5-dihydro-2-furoyl)-CoA. Methylene blue, nitro blue, tetrazolium and a membrane fraction from Pseudomonas putida can act as acceptors.
History
EC 1.3.99.8 created 1976
Pathway
ec00365  Furfural degradation
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
K16877  2-furoyl-CoA dehydrogenase large subunit
K16878  2-furoyl-CoA dehydrogenase FAD binding subunit
K16879  2-furoyl-CoA dehydrogenase 2Fe-2S iron sulfur subunit
Genes
PPSE: BN5_2298(hmfA) BN5_2299(hmfB) BN5_2300(hmfC)
PMAN: OU5_0887 OU5_0888 OU5_0889
PSTT: CH92_11530 CH92_11535 CH92_11540
PPUU: PputUW4_02623 PputUW4_02624 PputUW4_02625
PSIL: PMA3_09770 PMA3_09775 PMA3_09780
ADI: B5T_02845 B5T_02846 B5T_02847
RPI: Rpic_2052 Rpic_2053 Rpic_2054
RPF: Rpic12D_1744 Rpic12D_1745 Rpic12D_1746
RPJ: N234_37060 N234_37065 N234_37070
REH: H16_A1701(coxS3) H16_A1702(h16_A1702) H16_A1703(coxL3)
BPC: BPTD_0692
BPER: BN118_3020
BPET: B1917_0471
BPEU: Q425_4310
BPAR: BN117_0386
BAV: BAV2737(cutS)
LIM: L103DPR2_01708(cutL_3) L103DPR2_01710(kdhA)
HYB: Q5W_13110
HPSE: HPF_15720(cdhA) HPF_15725(kdhA) HPF_15730(cdhC)
RGA: RGR602_PA00038(coxM-2)
BJA: blr3533(cutL) blr3534(cutM) blr3535
AOL: S58_42710
MAQU: Maq22A_c13985(coxS) Maq22A_c13990(coxM) Maq22A_c13995(coxL)
RBM: TEF_08695
DSH: Dshi_3719(coxL) Dshi_3720(coxM) Dshi_3721(coxS)
RID: RIdsm_04272(cdhA) RIdsm_04273(cdhB) RIdsm_04274(cdhC_3)
SWI: Swit_0499
SPHD: HY78_24200
SMIC: SmB9_31320
AZL: AZL_a11000 AZL_a11010(cutM) AZL_a11020(xdhB)
SAY: TPY_2900(cutM)
SALU: DC74_1456
SALL: SAZ_07805
STRE: GZL_07759
SMAL: SMALA_0618
NCA: Noca_1489
NDK: I601_1311(kdhA)
PSIM: KR76_07345
SEN: SACE_4018
SACC: EYD13_13315(kdhA)
AMYY: YIM_29100(cdhC2)
PSEE: FRP1_20535
CWO: Cwoe_4071
HWA: HQ_1944A(coxL)
STO: STK_00470
SID: M164_0871
SIH: SiH_0725
PYR: P186_1143
POG: Pogu_1990
VDI: Vdis_0419
VMO: VMUT_1125
 » show all
Taxonomy
Reference
1  [PMID:4655411]
  Authors
Kitcher JP, Trudgill PW, Rees JS.
  Title
Purification and properties of 2-furoyl-coenzyme A hydroxylase from Pseudomonas putida F2.
  Journal
Biochem J 130:121-32 (1972)
DOI:10.1042/bj1300121
Other DBs
ExplorEnz - The Enzyme Database: 1.3.99.8
IUBMB Enzyme Nomenclature: 1.3.99.8
ExPASy - ENZYME nomenclature database: 1.3.99.8
UM-BBD (Biocatalysis/Biodegradation Database): 1.3.99.8
BRENDA, the Enzyme Database: 1.3.99.8
CAS: 9068-18-2

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