KEGG   ENZYME: 1.3.8.8Help
Entry
EC 1.3.8.8                  Enzyme                                 

Name
long-chain acyl-CoA dehydrogenase;
palmitoyl-CoA dehydrogenase;
palmitoyl-coenzyme A dehydrogenase;
long-chain acyl-coenzyme A dehydrogenase;
long-chain-acyl-CoA:(acceptor) 2,3-oxidoreductase;
ACADL (gene name).
Class
Oxidoreductases;
Acting on the CH-CH group of donors;
With a flavin as acceptor
BRITE hierarchy
Sysname
long-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase
Reaction(IUBMB)
a long-chain acyl-CoA + electron-transfer flavoprotein = a long-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein [RN:R00392]
Reaction(KEGG)
Substrate
long-chain acyl-CoA [CPD:C02843];
electron-transfer flavoprotein [CPD:C04253]
Product
long-chain trans-2,3-dehydroacyl-CoA;
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 from pig liver can accept substrates with acyl chain lengths of 6 to at least 16 carbon atoms. The highest activity was found with C12, and the rates with C8 and C16 were 80 and 70%, respectively [2]. The enzyme from rat can accept substrates with C8-C22. It is most active with C14 and C16, and has no activity with C4, C6 or C24 [4]. cf. EC 1.3.8.1, short-chain acyl-CoA dehydrogenase, EC 1.3.8.8, medium-chain acyl-CoA dehydrogenase, and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase.
History
EC 1.3.8.8 created 1989 as EC 1.3.99.13, part transferred 2012 to EC 1.3.8.8
Pathway
ec00071  Fatty acid degradation
ec01100  Metabolic pathways
Orthology
K00255  long-chain-acyl-CoA dehydrogenase
Genes
HSA: 33(ACADL)
PTR: 459914(ACADL)
PPS: 100986924(ACADL)
GGO: 101127206(ACADL)
PON: 100440170(ACADL)
NLE: 100595536(ACADL)
MCC: 711485(ACADL)
MCF: 102134056(ACADL)
CSAB: 103217758(ACADL)
RRO: 104655498(ACADL)
RBB: 108540361(ACADL)
CJC: 100414283(ACADL)
SBQ: 101034499(ACADL)
MMU: 11363(Acadl)
RNO: 25287(Acadl)
CGE: 100759026(Acadl)
NGI: 103744464(Acadl)
HGL: 101698104(Acadl)
CCAN: 109691994(Acadl)
OCU: 100358521(ACADL)
TUP: 102478785(ACADL)
CFA: 478895(ACADL)
AML: 100467341(ACADL)
UMR: 103659964(ACADL)
ORO: 101385517(ACADL)
FCA: 101098884(ACADL)
PTG: 102967046(ACADL)
AJU: 106984776
BTA: 614508(ACADL)
BOM: 102266624(ACADL)
BIU: 109570336(ACADL)
PHD: 102344708(ACADL)
CHX: 102176568(ACADL)
OAS: 101123271(ACADL)
SSC: 396931(ACADL)
CFR: 102511378(ACADL)
CDK: 105101591(ACADL)
BACU: 103002780(ACADL)
LVE: 103080374(ACADL)
OOR: 101280788(ACADL)
ECB: 100066893(ACADL)
EPZ: 103564161(ACADL)
EAI: 106848054(ACADL)
MYB: 102260528(ACADL)
MYD: 102757895(ACADL)
HAI: 109390442(ACADL)
RSS: 109445052(ACADL)
PALE: 102878971(ACADL)
LAV: 100657035(ACADL)
TMU: 101358665
MDO: 100015264(ACADL)
SHR: 100914644(ACADL)
OAA: 100077024(ACADL)
GGA: 424005(ACADL)
MGP: 100540388(ACADL)
CJO: 107316458(ACADL)
APLA: 101801335(ACADL)
ACYG: 106034509(ACADL)
TGU: 100224317(ACADL)
GFR: 102044703(ACADL)
FAB: 101817085(ACADL)
PHI: 102106512(ACADL)
PMAJ: 107207764(ACADL)
CCW: 104694536(ACADL)
FPG: 101924862(ACADL)
FCH: 102047187(ACADL)
CLV: 102095816(ACADL)
EGZ: 104124193(ACADL)
AAM: 106492331(ACADL)
ASN: 102387928(ACADL)
AMJ: 102565241(ACADL)
PSS: 102461956(ACADL)
CMY: 102941001(ACADL)
CPIC: 101943787(ACADL)
ACS: 100562130(acadl)
PVT: 110072389(ACADL)
PBI: 103062999(ACADL)
GJA: 107119083(ACADL)
XLA: 446669(acadl.L)
XTR: 734116(acadl)
NPR: 108794423(ACADL)
DRE: 394156(acadl)
SRX: 107747617(acadl)
SANH: 107700586(acadl)
SGH: 107576428
CCAR: 109108344
IPU: 108264529(acadl)
AMEX: 111197552(acadl)
TRU: 101075644(acadl)
LCO: 104929358(acadl)
NCC: 104953624(acadl)
MZE: 101469415(acadl)
OLA: 101159651(acadl)
XMA: 102229820(acadl) 106700234
NFU: 107377229(acadl)
LCF: 108873043(acadl)
HCQ: 109528476(acadl)
BPEC: 110170900
SASA: 106575817(acadl)
ELS: 105023135(acadl)
SFM: 108928934(acadl)
LCM: 102362263(ACADL)
CMK: 103182964(acadl)
CIN: 100180056
SPU: 577166
SKO: 100375371
CRG: 105333437
MYI: 110457184
LAK: 106173170
ABM: ABSDF1249
ABY: ABAYE0436(fadE) ABAYE1204 ABAYE2631(hcaD)
ACI: ACIAD1723(hcaD) ACIAD2226 ACIAD3191(fadE)
RDE: RD1_3970(fadE)
NAR: Saro_0132
MUL: MUL_3367(fadE20)
MVA: Mvan_2439
RER: RER_27750(fadE)
FAL: FRAAL0412
SEN: SACE_3993
RCA: Rcas_2461
 » show all
Taxonomy
Reference
1  [PMID:13239683]
  Authors
CRANE FL, HAUGE JG, BEINERT H
  Title
Flavoproteins involved in the first oxidative step of the fatty acid cycle.
  Journal
Biochim Biophys Acta 17:292-4 (1955)
DOI:10.1016/0006-3002(55)90374-7
Reference
2  [PMID:13319294]
  Authors
HAUGE JG, CRANE FL, BEINERT H.
  Title
On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A.  III.  Palmityl coA dehydrogenase.
  Journal
J Biol Chem 219:727-33 (1956)
Reference
3  [PMID:1015826]
  Authors
Hall CL, Heijkenskjold L, Bartfai T, Ernster L, Kamin H.
  Title
Acyl coenzyme A dehydrogenases and electron-transferring flavoprotein from beef hart mitochondria.
  Journal
Arch Biochem Biophys 177:402-14 (1976)
DOI:10.1016/0003-9861(76)90453-7
Reference
4  [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 260:1311-25 (1985)
  Sequence
[rno:25287]
Reference
5  [PMID:8155643]
  Authors
Djordjevic S, Dong Y, Paschke R, Frerman FE, Strauss AW, Kim JJ
  Title
Identification of the catalytic base in long chain acyl-CoA dehydrogenase.
  Journal
Biochemistry 33:4258-64 (1994)
Other DBs
ExplorEnz - The Enzyme Database: 1.3.8.8
IUBMB Enzyme Nomenclature: 1.3.8.8
ExPASy - ENZYME nomenclature database: 1.3.8.8
BRENDA, the Enzyme Database: 1.3.8.8
CAS: 59536-74-2

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