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 other, unknown, 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
Furfural degradation
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
PPUU: 
PSTT: 
ADI: 
RPI: 
RPF: 
RPJ: 
REU: 
REH: 
H16_A1701(coxS3) H16_A1702(h16_A1702) H16_A1703(coxL3)
BXE: 
BXB: 
BPH: 
BPY: 
BUG: 
BGE: 
BGF: 
BYI: 
BPX: 
AMIM: 
ACK: 
BJA: 
blr3533(cutL) blr3534(cutM) blr3535
BJU: 
RPC: 
MRD: 
MET: 
MNO: 
MOR: 
DSH: 
PTP: 
ACR: 
AMV: 
AZL: 
GKA: 
GMC: 
GGH: 
SVL: 
SRC: 
AMQ: 
PDX: 
PYR: 
 » 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 (1972) 121-32.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
UM-BBD (Biocatalysis/Biodegradation Database): 
BRENDA, the Enzyme Database: 
CAS: 
9068-18-2

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