KEGG   ENZYME: 2.1.1.145
Entry
EC 2.1.1.145                Enzyme                                 

Name
trans-aconitate 3-methyltransferase
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
Sysname
S-adenosyl-L-methionine:(E)-prop-1-ene-1,2,3-tricarboxylate 3'-O-methyltransferase
Reaction(IUBMB)
S-adenosyl-L-methionine + trans-aconitate = S-adenosyl-L-homocysteine + (E)-2-(methoxycarbonylmethyl)butenedioate [RN:R05764]
Reaction(KEGG)
R05764
Substrate
S-adenosyl-L-methionine [CPD:C00019];
trans-aconitate [CPD:C02341]
Product
S-adenosyl-L-homocysteine [CPD:C00021];
(E)-2-(methoxycarbonylmethyl)butenedioate [CPD:C11515]
Comment
Also catalyses the formation of the methyl monoester of cis-aconitate, isocitrate and citrate, but more slowly. While the enzyme from Saccharomyces cerevisiae forms (E)-2-(methoxycarbonylmethyl)butenedioate as the product, that from Escherichia coli forms (E)-3-(methoxycarbonyl)-pent-2-enedioate and is therefore classified as a separate enzyme (cf. EC 2.1.1.144, trans-aconitate 2-methyltransferase)
History
EC 2.1.1.145 created 2002
Orthology
K22438  trans-aconitate 3-methyltransferase
Genes
MDO: 100025184
PCW: 110198060
ASN: 102381625
AMJ: 102569370
PSS: 102451271
CMY: 102933461
CPIC: 101943168
XTR: 100498610
NPR: 108800554 108802257
DRE: 555292(zgc:162396)
SRX: 107733630
SANH: 107663909
CCAR: 109110971
EEE: 113592256
NCC: 104955817
NFU: 107389394
KMR: 108238497(zgc:162396)
ALIM: 106529443
AOCE: 111563024
HCQ: 109528745
BPEC: 110170910
MALB: 109968563
SASA: 106575799 106586297(Y3374) 106586299 106586300(Y3374)
SALP: 111976662
LCM: 102367000
BTAB: 109040316
PTEP: 107445017
MYI: 110453423
SCE: YER175C(TMT1)
KMX: KLMA_30285(TMT1)
NCS: NCAS_0A03100(NCAS0A03100) NCAS_0B04900(NCAS0B04900)
NDI: NDAI_0B02310(NDAI0B02310) NDAI_0I02680(NDAI0I02680)
TPF: TPHA_0A01900(TPHA0A01900)
TBL: TBLA_0C01350(TBLA0C01350) TBLA_0C01360(TBLA0C01360) TBLA_0F03870(TBLA0F03870)
TDL: TDEL_0G00510(TDEL0G00510) TDEL_0G00520(TDEL0G00520)
KAF: KAFR_0B02610(KAFR0B02610) KAFR_0B06440(KAFR0B06440) KAFR_0C00170(KAFR0C00170)
PIC: PICST_35256(TMT2) PICST_52120(TMT1)
CAL: CAALFM_C105830WA(CaO19.2468) CAALFM_C110310WA(CaO19.4902)
SLB: AWJ20_2280(TMT1)
NCR: NCU06616
NTE: NEUTE1DRAFT128461(NEUTE1DRAFT_128461)
SSCK: SPSK_02666
MAW: MAC_01281
MAJ: MAA_06303
CMT: CCM_00874
MBE: MBM_06649
ANG: ANI_1_576054(An06g02170)
PTE: PTT_10228
CNE: CNM00330
CNB: CNBM0330
 » show all
Reference
1  [PMID:10224113]
  Authors
Cai H, Clarke S
  Title
A novel methyltransferase catalyzes the methyl esterification of trans-aconitate in Escherichia coli.
  Journal
J Biol Chem 274:13470-9 (1999)
DOI:10.1074/jbc.274.19.13470
Reference
2  [PMID:11329290]
  Authors
Cai H, Strouse J, Dumlao D, Jung ME, Clarke S
  Title
Distinct reactions catalyzed by bacterial and yeast trans-aconitate methyltransferases.
  Journal
Biochemistry 40:2210-9 (2001)
DOI:10.1021/bi0022902
Other DBs
ExplorEnz - The Enzyme Database: 2.1.1.145
IUBMB Enzyme Nomenclature: 2.1.1.145
ExPASy - ENZYME nomenclature database: 2.1.1.145
BRENDA, the Enzyme Database: 2.1.1.145
CAS: 235107-12-7

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