Entry
Name
short-chain 2-methylacyl-CoA dehydrogenase;
ACADSB (gene name);
2-methylacyl-CoA dehydrogenase;
branched-chain acyl-CoA dehydrogenase (ambiguous);
2-methyl branched chain acyl-CoA dehydrogenase;
2-methylbutanoyl-CoA:(acceptor) oxidoreductase;
2-methyl-branched-chain-acyl-CoA:electron-transfer flavoprotein 2-oxidoreductase;
2-methyl-branched-chain-enoyl-CoA reductase
Class
Oxidoreductases;
Acting on the CH-CH group of donors;
With a flavin as acceptor
BRITE hierarchy
Sysname
short-chain 2-methylacyl-CoA:electron-transfer flavoprotein 2-oxidoreductase
Reaction(IUBMB)
2-methylbutanoyl-CoA + electron-transfer flavoprotein = (E)-2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+ [RN:
R03169 ]
Reaction(KEGG)
Substrate
2-methylbutanoyl-CoA [CPD:
C01033 ];
electron-transfer flavoprotein [CPD:
C04253 ]
Product
(E)-2-methylbut-2-enoyl-CoA [CPD:
C03345 ];
reduced electron-transfer flavoprotein [CPD:
C04570 ];
H+ [CPD:
C00080 ]
Comment
A flavoprotein (FAD). The mammalian enzyme catalyses an oxidative reaction as a step in the mitochondrial beta-oxidation of short-chain 2-methyl fatty acids and participates in isoleucine degradation. The enzyme from the parasitic helminth Ascaris suum catalyses a reductive reaction as part of a fermentation pathway, shuttling reducing power from the electron-transport chain to 2-methyl branched-chain enoyl CoA.
History
EC 1.3.8.5 created 1992 as EC 1.3.1.52, transferred 2012 to EC 1.3.8.5 (EC 1.3.99.12, created 1986, incorporated 2020), modified 2020
Pathway
ec00280 Valine, leucine and isoleucine degradation
ec01110 Biosynthesis of secondary metabolites
Orthology
K09478 short-chain 2-methylacyl-CoA dehydrogenase
K11410 short-chain 2-methylacyl-CoA dehydrogenase
Genes
LWW : 102728102 102737187(ACADSB)
BMUS : 118882335(ACADSB) 118898972
OOR : 101281709 101289781(ACADSB)
RFQ : 117018663 117036024(ACADSB)
DRE : 100037342 110437777(acadsb)
CAUA : 113055802 113055901
PPRM : 120487121(acadsb) 120487376
MASI : 127423528 127426662
CMAO : 118808980 118809021
PSWI : 130203621 130204053(acadsb)
SASA : 106575476 106577431
STRU : 115190109 115190110
OMY : 110511537 110531877 118966130
OGO : 124018349 124018350 124018361
CCLU : 121578415 123491660
PSPA : 121322435 121325972
DSI : Dsimw501_GD12323(Dsim_GD12323)
DYA : Dyak_GE22545 Dyak_GE22549
TDA : 119669255 119669866 119670213 119670214
AALB : 109407248 115258624
ASUA : 134212696 134212704
MPHA : 105829763 105836416
ACEP : 105618707 105620526
PPYR : 116163432 116163438
OTU : 111413217 111413219 111423491
MSEX : 115442043 119189779
CFEL : 113365686 113366333
CCRN : 123295741 123299743 123299932
NLU : 111045258 120351105 120351214 120351215
PHU : Phum_PHUM226870 Phum_PHUM226980
TPAL : 117646929 117647765
SGRE : 126275659 126320432
TUT : 107368035 107368037 107368406
CEL : CELE_C55B7.4(acdh-1) CELE_K06A5.6(acdh-3) CELE_T10E9.9(acdh-4)
CBR : CBG_12633 CBG_12644(Cbr-acdh-1) CBG_12664
CRQ : GCK72_002777 GCK72_002779 GCK72_002813 GCK72_002824 GCK72_002828 GCK72_002832 GCK72_002851
PMAX : 117320595 117339390
TAD : TRIADDRAFT_19851 TRIADDRAFT_20131 TRIADDRAFT_33900 TRIADDRAFT_58518
GSL : Gasu_17150 Gasu_59510
YLI : 2910175(YALI2_D00809g)
NTE : NEUTE1DRAFT145014(NEUTE1DRAFT_145014)
SMP : 10803883(SMAC4_04665)
TATV : 25777269(TrAtP1_007386)
TASP : 36618310(TrAFT101_007993)
MAW : 19248309(J3458_001253)
PLJ : 28888665(PLICBS_003834)
CDET : 87947172(CDEST_10672)
CPW : 9694367(D8B26_002845)
PNO : SNOG_14270(SNOG_14271)
PTRR : 6343082(PtrM4_118000)
CDEP : 91089990(L203_105781)
KMG : 30162999(I203_101990)
KNE : 92180254(IAR55_002996)
CCAC : CcaHIS019_0604440(CcaverHIS019_0604440)
ABP : AGABI1DRAFT116215(AGABI1DRAFT_116215)
ABV : AGABI2DRAFT191649(AGABI2DRAFT_191649)
SCM : SCHCO_02645843(SCHCODRAFT_02645843)
PGR : PGTG_06436 PGTG_13966
DDI : DDB_G0282967(acadsb)
FCY : FRACYDRAFT_187779(ACD2)
TPS : THAPSDRAFT_269127(ACD3)
PIF : PITG_06732 PITG_15615
PSOJ : PHYSODRAFT_350120 PHYSODRAFT_351306
BLAC : 94344363(CCR75_000585) 94347827(CCR75_004066)
LMAT : 92511168(LSCM1_01030)
LOI : 92357443(LSCM4_01456)
LEIS : 94176672(GH5_01053)
LENR : 94168324(CUR178_01038)
LEIN : 94184796(JIQ42_01047)
PHET : 94287394(JKF63_01269)
BLQ : L21SP5_00851(mmgC_1)
MTO : MTCTRI2_2546(fadE19)
MBO : BQ2027_MB2528C(fadE19)
MBM : BCGMEX_2512c(fadE19)
MSER : MTY59_34290(fadE19)
MMAE : MMARE11_37330(fadE19)
MBAI : MB901379_03415(mmgC_14)
MKY : IWGMT90018_19620(fadE19)
MPHL : MPHLCCUG_03665(acdA_10)
MSAL : DSM43276_04379(mmgC_10)
MTER : 4434518_01298(fadE19)
CAUS : CAURIC_08650(mmgC3)
TPUL : TPB0596_09180(fadE19)
SAMB : SAM23877_2814(yngJ)
SLE : sle_44610(sle_44610)
SRK : FGW37_11615 FGW37_30950
SSPO : DDQ41_07305 DDQ41_20970
SPAD : DVK44_10020 DVK44_31300
SHUN : DWB77_04913(mmgC_5)
SAKB : K1J60_03490 K1J60_28035
STAA : LDH80_10540 LDH80_25495
SXT : KPP03845_102934(mmgC_4)
KAB : B7C62_10610 B7C62_33350
AMAU : DSM26151_11630(bcd)
AMAV : GCM10025877_29910(fadE19)
PSUL : AU252_00840 AU252_01515 AU252_03420
BEI : GCM100_26030(fadE19)
NAQU : ENKNEFLB_01235(acdA_3)
FRI : FraEuI1c_1632 FraEuI1c_5336
AMQ : AMETH_1831(acdH) AMETH_5735(acdH)
ARHD : VSH64_03970 VSH64_25415 VSH64_28970
AMYZ : HUW46_05770(acdA_3)
ACAB : QRX50_15840 QRX50_42295
ACTU : Actkin_05414(mmgC_11)
ACTY : OG774_06525 OG774_23405
MCRA : ID554_14015 ID554_21250
ACTL : L3i22_000280 L3i22_023480
BALA : DSM104299_03850(bcd_2)
SBAE : DSM104329_00414(bcd)
» show all
Taxonomy
Reference
Authors
Ikeda Y, Dabrowski C, Tanaka K.
Title
Separation and properties of five distinct acyl-CoA dehydrogenases from rat liver mitochondria. Identification of a new 2-methyl branched chain acyl-CoA dehydrogenase.
Journal
J Biol Chem 258:1066-76 (1983)
Reference
Authors
Komuniecki R, Fekete S, Thissen-Parra J.
Title
Purification and characterization of the 2-methyl branched-chain Acyl-CoA dehydrogenase, an enzyme involved in NADH-dependent enoyl-CoA reduction in anaerobic mitochondria of the nematode, Ascaris suum.
Journal
J Biol Chem 260:4770-7 (1985)
Reference
Authors
Komuniecki R, McCrury J, Thissen J, Rubin N.
Title
Electron-transfer flavoprotein from anaerobic Ascaris suum mitochondria and its role in NADH-dependent 2-methyl branched-chain enoyl-CoA reduction.
Journal
Reference
Authors
Vockley J, Mohsen al-W A, Binzak B, Willard J, Fauq A.
Title
Mammalian branched-chain acyl-CoA dehydrogenases: molecular cloning and characterization of recombinant enzymes.
Journal
Reference
Authors
Andresen BS, Christensen E, Corydon TJ, Bross P, Pilgaard B, Wanders RJ, Ruiter JP, Simonsen H, Winter V, Knudsen I, Schroeder LD, Gregersen N, Skovby F
Title
Isolated 2-methylbutyrylglycinuria caused by short/branched-chain acyl-CoA dehydrogenase deficiency: identification of a new enzyme defect, resolution of its molecular basis, and evidence for distinct acyl-CoA dehydrogenases in isoleucine and valine metabolism.
Journal
Other DBs
ExplorEnz - The Enzyme Database: 1.3.8.5
ExPASy - ENZYME nomenclature database: 1.3.8.5
BRENDA, the Enzyme Database: 1.3.8.5