KEGG   ENZYME: 2.8.3.21
Entry
EC 2.8.3.21                 Enzyme                                 

Name
L-carnitine CoA-transferase;
CaiB;
crotonobetainyl/gamma-butyrobetainyl-CoA:carnitine CoA-transferase
Class
Transferases;
Transferring sulfur-containing groups;
CoA-transferases
Sysname
(E)-4-(trimethylammonio)but-2-enoyl-CoA:L-carnitine CoA-transferase
Reaction(IUBMB)
(1) (E)-4-(trimethylammonio)but-2-enoyl-CoA + L-carnitine = (E)-4-(trimethylammonio)but-2-enoate + L-carnitinyl-CoA [RN:R10643];
(2) 4-trimethylammoniobutanoyl-CoA + L-carnitine = 4-trimethylammoniobutanoate + L-carnitinyl-CoA [RN:R10644]
Reaction(KEGG)
R10643 R10644
Substrate
(E)-4-(trimethylammonio)but-2-enoyl-CoA [CPD:C20748];
L-carnitine [CPD:C00318];
4-trimethylammoniobutanoyl-CoA [CPD:C20749]
Product
(E)-4-(trimethylammonio)but-2-enoate [CPD:C04114];
L-carnitinyl-CoA [CPD:C20750];
4-trimethylammoniobutanoate [CPD:C01181]
Comment
The enzyme is found in gammaproteobacteria such as Proteus sp. and Escherichia coli. It has similar activity with both substrates.
History
EC 2.8.3.21 created 2014
Orthology
K08298  L-carnitine CoA-transferase
Genes
ECO: b0038(caiB)
ECJ: JW0037(caiB)
ECD: ECDH10B_0039(caiB)
EBW: BWG_0036(caiB)
ECOK: ECMDS42_0031(caiB)
ECE: Z0044(caiB)
ECS: ECs0041
ECF: ECH74115_0042(caiB)
ETW: ECSP_0041(caiB)
ELX: CDCO157_0040
EOI: ECO111_0039(caiB)
EOJ: ECO26_0039(caiB)
EOH: ECO103_0040(caiB)
ECOO: ECRM13514_0039(caiB)
ECOH: ECRM13516_0041(caiB)
ESL: O3K_21355
ESO: O3O_04030
ESM: O3M_21255
ECK: EC55989_0038(caiB)
ECG: E2348C_0039(caiB)
EOK: G2583_0040(caiB)
ELH: ETEC_0038
ECW: EcE24377A_0040(caiB)
EUN: UMNK88_38
ECP: ECP_0038
ENA: ECNA114_0025(caiB)
ECOS: EC958_0172(caiB)
ECV: APECO1_1943(caiB)
ECX: EcHS_A0042(caiB)
ECM: EcSMS35_0039(caiB)
ECY: ECSE_0039
ECR: ECIAI1_0040(caiB)
ECQ: ECED1_0037(caiB)
EUM: ECUMN_0040(caiB)
ECT: ECIAI39_0039(caiB)
EOC: CE10_0039(caiB)
ECI: UTI89_C0044(caiB)
EIH: ECOK1_0037(caiB)
ECZ: ECS88_0041(caiB)
ECC: c0047(caiB)
ELO: EC042_0040(caiB)
ESE: ECSF_0043
EKF: KO11_00190(caiB)
EAB: ECABU_c00430(caiB)
EDJ: ECDH1ME8569_0037(caiB)
ELW: ECW_m0038(caiB)
ELL: WFL_00190(caiB)
ELC: i14_0040(caiB)
ELD: i02_0040(caiB)
ELP: P12B_c0033(caiB)
ELF: LF82_0258(caiB)
ECOI: ECOPMV1_00039(caiB)
ECOJ: P423_00190
EFE: EFER_0046(caiB)
EAL: EAKF1_ch1384(caiB)
ESZ: FEM44_14685(caiB)
STY: STY0082(caiB)
STT: t0073(caiB)
STM: STM0072(caiB)
SEO: STM14_0085(caiB)
SEJ: STMUK_0073(caiB)
SEF: UMN798_0080(caiB)
SENR: STMDT2_00731(caiB)
SEND: DT104_00731(caiB)
SENI: CY43_00355
SPT: SPA0073(caiB)
SEK: SSPA0069
SEI: SPC_0077(caiB)
SEC: SCH_0066(caiB)
SHB: SU5_0707
SEW: SeSA_A0080(caiB)
SENS: Q786_00355
SED: SeD_A0078
SEG: SG0075(caiB)
SEL: SPUL_0077(caiB)
SEGA: SPUCDC_0077(caiB)
SET: SEN0073(caiB)
SENA: AU38_00355
SENO: AU37_00355
SENV: AU39_00355
SENQ: AU40_00390
SENL: IY59_00370
SEEP: I137_00335
SENB: BN855_750(caiB)
SENE: IA1_00365
SBG: SBG_0057(caiB)
SBZ: A464_60
SFL: SF0035(caiB)
SFX: S0037(caiB)
SFV: SFV_0032(caiB)
SFE: SFxv_0036(caiB)
SFN: SFy_0044
SFS: SFyv_0048
SFT: NCTC1_00035(caiB)
SDY: SDY_0060(caiB)
CRO: ROD_00401(caiB)
CKO: CKO_03345
CPOT: FOB25_07455(caiB)
CAMA: F384_00205
EBT: EBL_c33150(caiB)
METY: MRY16398_47850(caiB)
YRE: HEC60_04860(caiB)
PDZ: HHA33_24105(caiB)
EBF: D782_3831
PMR: PMI2656(caiB)
PMIB: BB2000_2647(caiB)
PHAU: PH4a_04755
PCIB: F9282_17055(caiB)
PCOL: F1325_16710(caiB)
PRG: RB151_007310(caiB)
PHEI: NCTC12003_00739(caiB)
PRQ: CYG50_11990(caiB)
ETR: ETAE_2662(caiB)
ETD: ETAF_2400
ETE: ETEE_0763
PRAG: EKN56_12485(caiB)
LRI: NCTC12151_02503(caiB)
SLO: Shew_2674
SSE: Ssed_3227
SPL: Spea_4036
SHL: Shal_0222
SWP: swp_4936
CPIN: CPIN18020_0492(caiB)
CRX: CRECT_1850(caiB)
AHS: AHALO_2625(caiB)
AMAR: AMRN_2724(caiB)
CSCI: HDCHBGLK_01434(baiF)
PHX: KGNDJEFE_00405(baiF)
DRM: Dred_0571
GOR: KTR9_0720
XYL: ET495_16525(caiB)
OEK: FFI11_010745(caiB)
PFR: PFREUD_02430(caiB)
PFRE: RM25_0221
AHE: Arch_1362
ARCA: HC352_07035(caiB)
TPYO: X956_03585
EYY: EGYY_03120(CaiB) EGYY_03150(CaiB) EGYY_17900(CaiB) EGYY_17980(CaiB) EGYY_27330(CaiB) EGYY_27410(CaiB)
GPA: GPA_25080
CBAC: JI75_07135
 » show all
Reference
1  [PMID:11409545]
  Authors
Engemann C, Elssner T, Kleber HP.
  Title
Biotransformation of crotonobetaine to L(-)-carnitine in Proteus sp.
  Journal
Arch Microbiol 175:353-9 (2001)
DOI:10.1007/s002030100272
  Sequence
[ag:CAD48580] [pmib:BB2000_2647] [pmr:PMI2656]
Reference
2  [PMID:11551212]
  Authors
Elssner T, Engemann C, Baumgart K, Kleber HP
  Title
Involvement of coenzyme A esters and two new enzymes, an enoyl-CoA hydratase and  a CoA-transferase, in the hydration of crotonobetaine to L-carnitine by Escherichia coli.
  Journal
Biochemistry 40:11140-8 (2001)
DOI:10.1021/bi0108812
  Sequence
[eco:b0038]
Reference
3  [PMID:15518548]
  Authors
Stenmark P, Gurmu D, Nordlund P
  Title
Crystal structure of CaiB, a type-III CoA transferase in carnitine metabolism.
  Journal
Biochemistry 43:13996-4003 (2004)
DOI:10.1021/bi048481c
  Sequence
[eco:b0038]
Reference
4  [PMID:15731894]
  Authors
Engemann C, Elssner T, Pfeifer S, Krumbholz C, Maier T, Kleber HP
  Title
Identification and functional characterisation of genes and corresponding enzymes involved in carnitine metabolism of Proteus sp.
  Journal
Arch Microbiol 183:176-89 (2005)
DOI:10.1007/s00203-005-0760-2
  Sequence
[ag:CAD48580] [pmib:BB2000_2647] [pmr:PMI2656]
Reference
5  [PMID:15823031]
  Authors
Rangarajan ES, Li Y, Iannuzzi P, Cygler M, Matte A
  Title
Crystal structure of Escherichia coli crotonobetainyl-CoA: carnitine CoA-transferase (CaiB) and its complexes with CoA and carnitinyl-CoA.
  Journal
Biochemistry 44:5728-38 (2005)
DOI:10.1021/bi047656f
  Sequence
[eco:b0038]
Other DBs
ExplorEnz - The Enzyme Database: 2.8.3.21
IUBMB Enzyme Nomenclature: 2.8.3.21
ExPASy - ENZYME nomenclature database: 2.8.3.21
BRENDA, the Enzyme Database: 2.8.3.21
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