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
ECOb0038(caiB)
ECJJW0037(caiB)
ECDECDH10B_0039(caiB)
EBWBWG_0036(caiB)
ECOKECMDS42_0031(caiB)
ECEZ0044(caiB)
ECSECs_0041(caiB)
ECFECH74115_0042(caiB)
ETWECSP_0041(caiB)
ELXCDCO157_0040
EOIECO111_0039(caiB)
EOJECO26_0039(caiB)
EOHECO103_0040(caiB)
ECOOECRM13514_0039(caiB)
ECOHECRM13516_0041(caiB)
ESLO3K_21355
ESOO3O_04030
ESMO3M_21255
ECKEC55989_0038(caiB)
ECGE2348C_0039(caiB)
EOKG2583_0040(caiB)
ELRECO55CA74_00190
ELHETEC_0038
ECWEcE24377A_0040(caiB)
EUNUMNK88_38
ECPECP_0038
ENAECNA114_0025(caiB)
ECOSEC958_0172(caiB)
ECVAPECO1_1943(caiB)
ECOAAPECO78_03650
ECXEcHS_A0042(caiB)
ECMEcSMS35_0039(caiB)
ECYECSE_0039
ECRECIAI1_0040(caiB)
ECQECED1_0037(caiB)
EUMECUMN_0040(caiB)
ECTECIAI39_0039(caiB)
EOCCE10_0039(caiB)
ECIUTI89_C0044(caiB)
EIHECOK1_0037(caiB)
ECZECS88_0041(caiB)
ECCc0047(caiB)
ELOEC042_0040(caiB)
ELNNRG857_00200
ESEECSF_0043
ECLEcolC_3617
EKOEKO11_3874
EKFKO11_00190(caiB)
EABECABU_c00430(caiB)
EDHEcDH1_3561
EDJECDH1ME8569_0037(caiB)
ELUUM146_22970
ELWECW_m0038(caiB)
ELLWFL_00190(caiB)
ELCi14_0040(caiB)
ELDi02_0040(caiB)
ELPP12B_c0033(caiB)
ELFLF82_0258(caiB)
ECOLLY180_00195
ECOIECOPMV1_00039(caiB)
ECOJP423_00190
EFEEFER_0046(caiB)
EALEAKF1_ch1384(caiB)
EMAC1192_12785
ESZFEM44_14685(caiB)
STYSTY0082(caiB)
STTt0073(caiB)
SEXSTBHUCCB_830
SENTTY21A_00375
STMSTM0072(caiB)
SEOSTM14_0085(caiB)
SEVSTMMW_00741
SEMSTMDT12_C00730
SEJSTMUK_0073(caiB)
SEFUMN798_0080(caiB)
SETUSTU288_00360
SETCCFSAN001921_17060
SENRSTMDT2_00731(caiB)
SENDDT104_00731(caiB)
SENICY43_00355
SEENSE451236_06370
SPTSPA0073(caiB)
SEKSSPA0069
SPQSPAB_00088
SEISPC_0077(caiB)
SECSCH_0066(caiB)
SEHSeHA_C0076
SHBSU5_0707
SENHCFSAN002069_08870
SEEHSEEH1578_09390
SEESNSL254_A0076
SENNSN31241_10510
SEWSeSA_A0080(caiB)
SEASeAg_B0079
SENSQ786_00355
SEDSeD_A0078
SEGSG0075(caiB)
SELSPUL_0077(caiB)
SEGASPUCDC_0077(caiB)
SETSEN0073(caiB)
SENAAU38_00355
SENOAU37_00355
SENVAU39_00355
SENQAU40_00390
SENLIY59_00370
SENJCFSAN001992_10665
SEECCFSAN002050_06810
SEEBSEEB0189_019025
SEEPI137_00335
SENBBN855_750(caiB)
SENEIA1_00365
SENCSEET0819_07250
SESSARI_02928
SBGSBG_0057(caiB)
SBZA464_60
SBVN643_00275
SALZEOS98_18880
SFLSF0035(caiB)
SFXS0037(caiB)
SFVSFV_0032(caiB)
SFESFxv_0036(caiB)
SFNSFy_0044
SFSSFyv_0048
SFTNCTC1_00035(caiB)
SDYSDY_0060(caiB)
SDZAsd1617_00065
CROROD_00401(caiB)
CKOCKO_03345
CFDCFNIH1_09900
CBRAA6J81_13210
CWECO701_18220
CYOCD187_20360
CPOTFOB25_07455(caiB)
CFQC2U38_03520
CSEDJY391_18145(caiB)
CAMAF384_00205
CAFAL524_22260
CIFAL515_04995
CFARCI104_04645
CIRC2U53_04685
CIEAN232_26290
CPARCUC49_00185
CTELGBC03_25650(caiB)
CITZE4Z61_13395(caiB)
CARSE1B03_04735(caiB)
EBTEBL_c33150(caiB)
ESCEntcl_2476
KLEAO703_09855
METYMRY16398_47850(caiB)
ASUBNLZ15_03195(caiB)
YREHEC60_04860(caiB)
KINAB182_21540
PDZHHA33_24105(caiB)
PSGCG163CM_28650(caiB)
EBFD782_3831
EBCC2U52_03235
PMRPMI2656(caiB)
PMIBBB2000_2647(caiB)
PVLAOB99_14515
PVGCRN77_06410
PHAUPH4a_04755
PROTBTA34_14495
PCOLF1325_16710(caiB)
PCIBF9282_17055(caiB)
PPEEI6G31_11895(caiB)
PRGRB151_007310(caiB)
PHEINCTC12003_00739(caiB)
PRQCYG50_11990(caiB)
EICNT01EI_2958
ETRETAE_2662(caiB)
ETDETAF_2400
ETEETEE_0763
ETCETAC_12790
EDWQY76_07185
EDLAAZ33_14080(caiB)
EHOA9798_03960
HAVAT03_19295
HPARAL518_07300
OPODSM2777_06090
LPVHYN51_05070
PRAGEKN56_12485(caiB)
LRINCTC12151_02503(caiB)
SLOShew_2674
SSESsed_3227
SPLSpea_4036
SHLShal_0222
SWPswp_4936
SALGBS332_05365
SLJEGC82_18070
SCAATUM17387_35770(caiB)
CPINCPIN18020_0492(caiB)
CRXCRECT_1850(caiB)
AHSAHALO_2625(caiB)
AMARAMRN_2724(caiB)
PBIZLWC08_01455(caiB)
BACIB1NLA3E_21280
CSCIHDCHBGLK_01434(baiF)
PHXKGNDJEFE_00405(baiF)
DSYDSY0941 DSY4297 DSY4305
DHDDhaf_0307 Dhaf_1018 Dhaf_1026 Dhaf_4597 Dhaf_4607
DDHDesde_0936 Desde_0944
DMTDESME_10090 DESME_10120
DRMDred_0571
GORKTR9_0720
XYLET495_16525(caiB)
OEKFFI11_010745(caiB)
GYUFE374_07890(caiB)
PFRPFREUD_02430(caiB)
PFRERM25_0221
AHEArch_1362
ARCAHC352_07035(caiB)
TPYCQ11_04200
TPYOX956_03585
TPECHLG82_02700(caiB)
ACTTDDD63_04070
AMYADJ76_00880
FSLEJO69_02445
ELEElen_1833 Elen_2883 Elen_2886
EYYEGYY_03120(CaiB) EGYY_03150(CaiB) EGYY_17900(CaiB) EGYY_17980(CaiB) EGYY_27330(CaiB) EGYY_27410(CaiB)
EGDGS424_010365(caiB) GS424_016620 GS424_016635
GPAGPA_25080
AHATADCFC_03550 ADCFC_03590 ADCFC_16300
CBACJI75_07135
RTSCE91St31_10340
 » 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
LinkDB

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