KEGG   ENZYME: 5.4.99.13Help
Entry
EC 5.4.99.13                Enzyme                                 

Name
isobutyryl-CoA mutase;
isobutyryl coenzyme A mutase;
butyryl-CoA:isobutyryl-CoA mutase;
icmA (gene name);
icmB (gene name);
icmF (gene name)
Class
Isomerases;
Intramolecular transferases;
Transferring other groups
BRITE hierarchy
Sysname
2-methylpropanoyl-CoA CoA-carbonylmutase
Reaction(IUBMB)
2-methylpropanoyl-CoA = butanoyl-CoA [RN:R01181]
Reaction(KEGG)
Substrate
2-methylpropanoyl-CoA [CPD:C00630]
Product
butanoyl-CoA [CPD:C00136]
Comment
This bacterial enzyme utilizes 5'-deoxyadenosylcobalamin as a cofactor. Following substrate binding, the enzyme catalyses the homolytic cleavage of the cobalt-carbon bond of AdoCbl, yielding cob(II)alamin and a 5'-deoxyadenosyl radical, which initiates the the carbon skeleton rearrangement reaction by hydrogen atom abstraction from the substrate. At the end of each catalytic cycle the 5'-deoxyadenosyl radical and cob(II)alamin recombine, regenerating the resting form of the cofactor. The enzyme is prone to inactivation resulting from occassional loss of the 5'-deoxyadenosyl molecule. Inactivated enzymes are repaired by the action of EC 2.5.1.17, cob(I)yrinic acid a,c-diamide adenosyltransferase, and a G-protein chaperone, which restore cob(II)alamin (which is first reduced to cob(I)alamin by an unidentified reductase) to 5'-deoxyadenosylcobalamin and load it back on the mutase. Some mutases are fused with their G-protein chaperone. These enzyme can also catalyse the interconversion of isovaleryl-CoA with pivalyl-CoA.
History
EC 5.4.99.13 created 1992, revised 2017
Orthology
K11942  isobutyryl-CoA mutase
Genes
XSA: SB85_06415
XTN: FD63_05995
SACZ: AOT14_13180
STEK: AXG53_11455
PSU: Psesu_1629
PSUW: WQ53_15300
LAB: LA76x_3173
LAQ: GLA29479_11
LCP: LC55x_3186
LGU: LG3211_2045
LEZ: GLE_1980(mutA)
LEM: LEN_3025(mcmA)
DKO: I596_1202
MVS: MVIS_1782
MYA: MORIYA_0502(icmF)
CYQ: Q91_1545
NOC: Noc_1893
NHL: Nhal_2497
PSPI: PS2015_869
RSO: RSc0237
RSN: RSPO_c03163(sbm)
RSE: F504_254
RPI: Rpic_0089
REH: H16_A0280(sbm1)
CNC: CNE_1c02900(sbm)
RME: Rmet_0210(sbm)
CGD: CR3_0214
BXE: Bxe_A4277
BXB: DR64_1955
BPH: Bphy_0156
RFR: Rfer_3612
POL: Bpro_4054
PNA: Pnap_3524
RTA: Rta_10110
LIM: L103DPR2_00610(scpA_1)
LIH: L63ED372_00087(scpA_1)
HYB: Q5W_17245
CBAA: SRAA_1743
CBAB: SMCB_1714
MPT: Mpe_A0903
LCH: Lcho_3844
TIN: Tint_2187
THI: THI_2523
RGE: RGE_43760
EBA: ebA3766
DSU: Dsui_1105
DAR: Daro_0243
AZO: azo0696
AZA: AZKH_4043
AOA: dqs_0766
TCL: Tchl_1708
GME: Gmet_1722
GUR: Gura_1342
GBM: Gbem_2838
GEM: GM21_1375
GEB: GM18_1282
DEU: DBW_0031
DOL: Dole_2188
DML: Dmul_11530(mcmL)
DAL: Dalk_2754
DAT: HRM2_10030(mcmL)
DTO: TOL2_C06760(mcmL)
MXA: MXAN_2261
CCX: COCOR_06686(sbm)
DBR: Deba_0776
BBA: Bd1853
BBAT: Bdt_1825
BBW: BDW_08170
BBAC: EP01_05350
BEX: A11Q_1097
BMX: BMS_3379
BHA: BH3796
BMQ: BMQ_5180
BMD: BMD_5166
BMEG: BG04_2174
BAG: Bcoa_1424
BMET: BMMGA3_16155(mutB2)
BACO: OXB_1405
BEO: BEH_23560
BKW: BkAM31D_24640(scpA_3)
BBEV: BBEV_0155(mutB)
GKA: GK3391
GTN: GTNG_3336
GGH: GHH_c34870(mutB2)
GEA: GARCT_03375(scpA_3)
AFL: Aflv_2734
AAMY: GFC30_336
LSP: Bsph_0976
HHD: HBHAL_4636(mcm1)
BSE: Bsel_3186
ASOC: CB4_00559(scpA_1)
BTS: Btus_1053
SIV: SSIL_3403
JEO: JMA_30540
HMO: HM1_0899(mutB)
NFA: NFA_10360
NFR: ERS450000_03079(scpA_2)
SCB: SCAB_6731
SBH: SBI_00608
SALS: SLNWT_6927
SERJ: SGUI_0766
NCA: Noca_4143
NDK: I601_1647(scpA_1)
PSIM: KR76_24415
MGG: MPLG2_0425(icmF)
TFU: Tfu_2811
TCU: Tcur_1029
SRO: Sros_3556
FAL: FRAAL5865(mcm)
GOB: Gobs_2225
MMAR: MODMU_5259
AMD: AMED_2498(mcm)
AMN: RAM_12700
AMM: AMES_2471(mcm)
AMZ: B737_2472(mcm)
AOI: AORI_2461
AMQ: AMETH_4866(mcm)
PDX: Psed_4409
PSEA: WY02_26050
PSEE: FRP1_16895
PSEH: XF36_16385
AMI: Amir_2277
SESP: BN6_32830
KAL: KALB_3062
ALL: CRK57417
TBI: Tbis_1618
CWO: Cwoe_2289
WCH: wcw_0462(mcm)
LIL: LA_2956
LIE: LIF_A2404
LIC: LIC_11105(mcm1)
LIS: LIL_12525(sbm)
LBJ: LBJ_2060
LBF: LBF_3084
LST: LSS_01872
GAU: GAU_2108
BLQ: L21SP5_02883(scpA_2)
MBAS: ALGA_3861
SRU: SRU_1689
SRM: SRM_01894(bhbA)
RMR: Rmar_0923
CPI: Cpin_1068
FLN: FLA_5249
SGN: SGRA_1904
PHE: Phep_1164
MUC: MuYL_4032
MGOT: MgSA37_04235(scpA_2)
SLI: Slin_2256
FAE: FAES_2675
HSW: Hsw_2041
FLM: MY04_0175
GFO: GFO_0483
GFL: GRFL_2313
FJO: Fjoh_2332
FJG: BB050_00315(scpA_1)
FPS: FP1940
FIN: KQS_06400
ZPR: ZPR_3143
CBAL: M667_19390
CBAT: M666_19330
DOK: MED134_03589(bhbA)
DDO: I597_2470(scpA_2)
MLT: VC82_506
NDO: DDD_2639
EAO: BD94_0244
ELB: VO54_02353(scpA_2)
MPW: MPR_1529
CHZ: CHSO_4564
CTAK: 4412677_01335(scpA)
WIN: WPG_0356
TMAR: MARIT_2504
AALG: AREALGSMS7_04828(icmF)
KOS: KORDIASMS9_04464(icmF)
MARF: CJ739_2784
FBA: FIC_02231
 » show all
Taxonomy
Reference
1
  Authors
Brendelberger, G., Retey, J., Ashworth, D.M., Reynolds, K., Willenbrock, F. and Robinson, J.A.
  Title
The enzymic interconversion of isobutyryl and N-butyrylcarba(dethia)-coenzyme-A - a coenzyme-B12-dependent carbon skeleton rearrangement.
  Journal
Angew Chem Int Ed Engl 27:1089-1091 (1988)
Reference
2  [PMID:10531377]
  Authors
Ratnatilleke A, Vrijbloed JW, Robinson JA.
  Title
Cloning and sequencing of the coenzyme B(12)-binding domain of isobutyryl-CoA mutase from Streptomyces cinnamonensis, reconstitution of mutase activity, and characterization of the recombinant enzyme produced in Escherichia coli.
  Journal
J Biol Chem 274:31679-85 (1999)
DOI:10.1074/jbc.274.44.31679
Reference
3  [PMID:19864421]
  Authors
Cracan V, Padovani D, Banerjee R
  Title
IcmF is a fusion between the radical B12 enzyme isobutyryl-CoA mutase and its G-protein chaperone.
  Journal
J Biol Chem 285:655-66 (2010)
DOI:10.1074/jbc.M109.062182
  Sequence
[gka:GK3391] [nfa:NFA_10360] [bxe:Bxe_A4277]
Reference
4  [PMID:22167181]
  Authors
Cracan V, Banerjee R
  Title
Novel coenzyme B12-dependent interconversion of isovaleryl-CoA and pivalyl-CoA.
  Journal
J Biol Chem 287:3723-32 (2012)
DOI:10.1074/jbc.M111.320051
  Sequence
[rme:Rmet_0210] [gka:GK3391]
Reference
5  [PMID:26318610]
  Authors
Jost M, Born DA, Cracan V, Banerjee R, Drennan CL
  Title
Structural Basis for Substrate Specificity in Adenosylcobalamin-dependent Isobutyryl-CoA Mutase and Related Acyl-CoA Mutases.
  Journal
J Biol Chem 290:26882-98 (2015)
DOI:10.1074/jbc.M115.676890
  Sequence
[rme:Rmet_0210]
Reference
6  [PMID:28130442]
  Authors
Li Z, Kitanishi K, Twahir UT, Cracan V, Chapman D, Warncke K, Banerjee R
  Title
Cofactor Editing by the G-protein Metallochaperone Domain Regulates the Radical B12 Enzyme IcmF.
  Journal
J Biol Chem 292:3977-3987 (2017)
DOI:10.1074/jbc.M117.775957
  Sequence
[rme:Rmet_0210]
Other DBs
ExplorEnz - The Enzyme Database: 5.4.99.13
IUBMB Enzyme Nomenclature: 5.4.99.13
ExPASy - ENZYME nomenclature database: 5.4.99.13
BRENDA, the Enzyme Database: 5.4.99.13
CAS: 116405-23-3

DBGET integrated database retrieval system