KEGG   ENZYME: 1.3.8.1Help
Entry
EC 1.3.8.1                  Enzyme                                 

Name
short-chain acyl-CoA dehydrogenase;
butyryl-CoA dehydrogenase;
butanoyl-CoA dehydrogenase;
butyryl dehydrogenase;
unsaturated acyl-CoA reductase;
ethylene reductase;
enoyl-coenzyme A reductase;
unsaturated acyl coenzyme A reductase;
butyryl coenzyme A dehydrogenase;
short-chain acyl CoA dehydrogenase;
short-chain acyl-coenzyme A dehydrogenase;
3-hydroxyacyl CoA reductase;
butanoyl-CoA:(acceptor) 2,3-oxidoreductase;
ACADS (gene name).
Class
Oxidoreductases;
Acting on the CH-CH group of donors;
With a flavin as acceptor
BRITE hierarchy
Sysname
short-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase
Reaction(IUBMB)
a short-chain acyl-CoA + electron-transfer flavoprotein = a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein [RN:R01178]
Reaction(KEGG)
Substrate
short-chain acyl-CoA [CPD:C20675];
electron-transfer flavoprotein [CPD:C04253]
Product
short-chain trans-2,3-dehydroacyl-CoA [CPD:C20676];
reduced electron-transfer flavoprotein [CPD:C04570]
Comment
Contains FAD as prosthetic group. One of several enzymes that catalyse the first step in fatty acids beta-oxidation. The enzyme catalyses the oxidation of saturated short-chain acyl-CoA thioesters to give a trans 2,3-unsaturated product by removal of the two pro-R-hydrogen atoms. The enzyme from beef liver accepts substrates with acyl chain lengths of 3 to 8 carbon atoms. The highest activity was reported with either butanoyl-CoA [2] or pentanoyl-CoA [4]. The enzyme from rat has only 10% activity with hexanoyl-CoA (compared to butanoyl-CoA) and no activity with octanoyl-CoA [6]. cf. EC 1.3.8.7, medium-chain acyl-CoA dehydrogenase, EC 1.3.8.8, long-chain acyl-CoA dehydrogenase, and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase.
History
EC 1.3.8.1 created 1961 as EC 1.3.2.1, transferred 1964 to EC 1.3.99.2, transferred 2011 to EC 1.3.8.1, modified 2012
Pathway
Fatty acid degradation
Valine, leucine and isoleucine degradation
Butanoate metabolism
Metabolic pathways
Biosynthesis of secondary metabolites
Orthology
K00248  
butyryl-CoA dehydrogenase
Genes
HSA: 
35(ACADS)
PTR: 
742921(ACADS)
PPS: 
100994372(ACADS)
GGO: 
101139640(ACADS)
PON: 
100172331(ACADS)
MCC: 
698196(ACADS)
MCF: 
102116240(ACADS)
MMU: 
11409(Acads)
RNO: 
64304(Acads)
CGE: 
100774097(Acads)
HGL: 
101722158(Acads)
TUP: 
102494372(ACADS)
CFA: 
477517(ACADS)
AML: 
FCA: 
101082442(ACADS)
PTG: 
102956610(ACADS)
BTA: 
511222(ACADS)
BOM: 
102269247(ACADS)
PHD: 
102337341(ACADS)
CHX: 
102180069(ACADS)
SSC: 
396932(ACADS)
CFR: 
102503720(ACADS)
ECB: 
100147113(ACADS)
MYB: 
102250514(ACADS)
MYD: 
102760180(ACADS)
PALE: 
102891595(ACADS)
MDO: 
100025804(ACADS)
SHR: 
100917746(ACADS)
OAA: 
100090404(ACADS)
GGA: 
416969(ACADS)
MGP: 
TGU: 
100232428(ACADS)
FAB: 
101818866(ACADS)
PHI: 
102112248(ACADS)
APLA: 
101801937(ACADS)
FPG: 
101913588(ACADS)
FCH: 
102052397(ACADS)
CLV: 
102088733(ACADS)
ASN: 
102368188(ACADS)
PSS: 
102460079(ACADS)
ACS: 
XLA: 
380563(acads)
XTR: 
394882(acads)
DRE: 
445288(acads)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
102355418(ACADS)
BFO: 
CIN: 
SPU: 
DME: 
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
AGA: 
AAG: 
CQU: 
AME: 
411697(Arc42)
NVI: 
100123507(Acads)
TCA: 
BMOR: 
API: 
PHU: 
ISC: 
NVE: 
MBR: 
PTI: 
TPS: 
PIF: 
EHX: 
GTT: 
PAE: 
PAU: 
PAP: 
PAG: 
PAF: 
PNC: 
PDK: 
PSG: 
PRP: 
PAEP: 
PAER: 
PAEM: 
PAEL: 
PAES: 
PPU: 
PPG: 
PPW: 
PPT: 
PPB: 
PPI: 
PPX: 
T1E_1162(acad8)
PPUH: 
PPUT: 
PPUN: 
PPUU: 
PST: 
PSB: 
PSP: 
PFL: 
PPRC: 
PFO: 
PFS: 
PFE: 
PFC: 
PPZ: 
PEN: 
PMY: 
PMK: 
PSA: 
PSZ: 
PSR: 
PSC: 
PSJ: 
PSH: 
PBA: 
PFV: 
PDR: 
PRE: 
PSV: 
PSK: 
PMON: 
PMOT: 
PCR: 
PRW: 
SFR: 
SLO: 
PAT: 
MAQ: 
MHC: 
MAD: 
MBS: 
AMC: 
AMAC: 
AMB: 
AMG: 
AMH: 
AMK: 
AMAA: 
AMAL: 
AMAE: 
AMAO: 
AMAD: 
AMAI: 
ALT: 
GAG: 
GNI: 
GPS: 
LPF: 
LPP: 
ABO: 
TOL: 
SAGA: 
RSO: 
RSC: 
RSL: 
RSN: 
RPI: 
RPF: 
REU: 
REH: 
RME: 
BUR: 
BPY: 
BUG: 
RFR: 
POL: 
AAV: 
AJS: 
DIA: 
AAA: 
VEI: 
DAC: 
DEL: 
VAP: 
VPE: 
CTT: 
ADN: 
ADK: 
RTA: 
MPT: 
HAR: 
TIN: 
GME: 
GUR: 
GBM: 
GEO: 
GEM: 
GEB: 
BBA: 
BMX: 
DPR: 
DAL: 
DAT: 
ADE: 
ACP: 
AFW: 
ANK: 
MXA: 
MFU: 
MSD: 
CCX: 
SUR: 
SCL: 
SCU: 
HOH: 
SFU: 
BMB: 
BJA: 
BRA: 
BBT: 
RPE: 
NHA: 
MEX: 
MEA: 
SIT: 
RDE: 
HBA: 
SJP: 
ACR: 
RRU: 
RCE: 
TMO: 
PBR: 
BCZ: 
BCZK5042(mmgC)
BTK: 
BTL: 
BCL: 
OIH: 
EAT: 
LBR: 
LBH: 
CRN: 
CAC: 
CAE: 
CPE: 
CPE2300(bcd)
CPF: 
CPR: 
CTC: 
CNO: 
CBO: 
CBO3199(bcd)
CBA: 
CBH: 
CBY: 
CBL: 
CBK: 
CBB: 
CBI: 
CBN: 
CBT: 
CBF: 
CBE: 
CKL: 
CKR: 
CCB: 
CLS: 
AMT: 
AOE: 
BPB: 
RHO: 
CSH: 
CDF: 
CDC: 
CDL: 
CST: 
SWO: 
DSY: 
DHD: 
DRM: 
PTH: 
PTH_0015(CaiA) PTH_0513(CaiA) PTH_1769(CaiA)
APR: 
ERE: 
ELM: 
OVA: 
OBV_03770(acdA) OBV_16240(acdA) OBV_28830(acdA) OBV_33360(acdA) OBV_40740(acdA)
TTE: 
TTE0545(CaiA)
CHY: 
CHY_1602(bcd3)
NTH: 
MAV: 
MVA: 
MGI: 
MSP: 
MMC: 
MKM: 
MJL: 
ASD: 
NFA: 
nfa24470(fadE24)
RHA: 
GBR: 
TPR: 
NCA: 
TFU: 
NDA: 
TCU: 
FRA: 
FRI: 
FAL: 
ACE: 
GOB: 
PDX: 
MAU: 
MIL: 
RXY: 
BHY: 
BRM: 
BPO: 
ABA: 
ACA: 
SUS: 
FNU: 
IPO: 
PGI: 
PG1076(acdA)
PGN: 
PAH: 
OSP: 
HHY: 
SLI: 
RSI: 
FBC: 
DRA: 
DGE: 
DDR: 
TTH: 
TTJ: 
MRB: 
TLE: 
TME: 
TAF: 
FNO: 
CEX: 
DDF: 
CNI: 
FSI: 
PIS: 
PCL: 
PAS: 
 » show all
Taxonomy
Reference
1  [PMID:13130522]
  Authors
MAHLER HR.
  Title
Studies on the fatty acid oxidizing system of animal tissues. IV. The prosthetic group of butyryl coenzyme A dehydrogenase.
  Journal
J. Biol. Chem. 206 (1954) 13-26.
Reference
2  [PMID:13130521]
  Authors
GREEN DE, MII S, MAHLER HR, BOCK RM
  Title
Studies on the fatty acid oxidizing system of animal tissues. III. Butyryl coenzyme A dehydrogenase.
  Journal
J. Biol. Chem. 206 (1954) 1-12.
Reference
3
  Authors
Beinert, H.
  Title
Acyl coenzyme A dehydrogenase.
  Journal
In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 447-466.
Reference
4  [PMID:6712627]
  Authors
Shaw L, Engel PC
  Title
The purification and properties of ox liver short-chain acyl-CoA dehydrogenase.
  Journal
Biochem. J. 218 (1984) 511-20.
Reference
5  [PMID:7601336]
  Authors
Thorpe C, Kim JJ
  Title
Structure and mechanism of action of the acyl-CoA dehydrogenases.
  Journal
FASEB. J. 9 (1995) 718-25.
Reference
6  [PMID:3968063]
  Authors
Ikeda Y, Okamura-Ikeda K, Tanaka K.
  Title
Purification and characterization of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and conversion of the apoenzyme to the holoenzyme.
  Journal
J. Biol. Chem. 260 (1985) 1311-25.
Reference
7  [PMID:16024185]
  Authors
McMahon B, Gallagher ME, Mayhew SG
  Title
The protein coded by the PP2216 gene of Pseudomonas putida KT2440 is an acyl-CoA  dehydrogenase that oxidises only short-chain aliphatic substrates.
  Journal
FEMS. Microbiol. Lett. 250 (2005) 121-7.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
UM-BBD (Biocatalysis/Biodegradation Database): 
BRENDA, the Enzyme Database: 
CAS: 
9027-88-7

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