KEGG   ENZYME: 2.8.3.21Help
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
BRITE hierarchy
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)
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
EOJ: ECO26_0039(caiB)
EOI: ECO111_0039(caiB)
EOH: ECO103_0040(caiB)
ECG: E2348C_0039(caiB)
EOK: G2583_0040(caiB)
ECC: c0047(caiB)
ECP: ECP_0038
ECI: UTI89_C0044(caiB)
ECV: APECO1_1943(caiB)
ECX: EcHS_A0042(caiB)
ECW: EcE24377A_0040(caiB)
ECM: EcSMS35_0039(caiB)
ECY: ECSE_0039
ECR: ECIAI1_0040(caiB)
ECQ: ECED1_0037(caiB)
ECK: EC55989_0038(caiB)
ECT: ECIAI39_0039(caiB)
EOC: CE10_0039(caiB)
EUM: ECUMN_0040(caiB)
ECZ: ECS88_0041(caiB)
ELO: EC042_0040(caiB)
ELH: ETEC_0038
ESE: ECSF_0043
ESO: O3O_04030
ESM: O3M_21255
ESL: O3K_21355
EKF: KO11_00190(caiB)
EAB: ECABU_c00430(caiB)
EDJ: ECDH1ME8569_0037(caiB)
EIH: ECOK1_0037(caiB)
ENA: ECNA114_0025(caiB)
EUN: UMNK88_38
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
ECOO: ECRM13514_0039(caiB)
ECOH: ECRM13516_0041(caiB)
ECOS: EC958_0172(caiB)
EFE: EFER_0046(caiB)
EAL: EAKF1_ch1384(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)
CKO: CKO_03345
CRO: ROD_00401(caiB)
CAMA: F384_00205
EBT: EBL_c33150(caiB)
EBF: D782_3831
PMR: PMI2656(caiB)
PMIB: BB2000_2647(caiB)
PRG: RB151_007310(caiB)
ETR: ETAE_2662(caiB)
ETD: ETAF_2400
ETE: ETEE_0763
SLO: Shew_2674
SSE: Ssed_3227
SPL: Spea_4036
SHL: Shal_0222
SWP: swp_4936
CPIN: CPIN18020_0492(caiB)
DSY: DSY4297
DHD: Dhaf_1026
DRM: Dred_0571
GOR: KTR9_0720
PFR: PFREUD_02430(caiB)
AHE: Arch_1362
TPYO: X956_03585
ELE: Elen_1833
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
Taxonomy
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 (2001) 353-9.
  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 (2001) 11140-8.
  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 (2004) 13996-4003.
  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 (2005) 176-89.
  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 (2005) 5728-38.
  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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