KEGG   ENZYME: 2.1.1.273Help
Entry
EC 2.1.1.273                Enzyme                                 

Name
benzoate O-methyltransferase;
BAMT;
S-adenosyl-L-methionine:benzoic acid carboxyl methyltransferase
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
BRITE hierarchy
Sysname
S-adenosyl-L-methionine:benzoate O-methyltransferase
Reaction(IUBMB)
S-adenosyl-L-methionine + benzoate = S-adenosyl-L-homocysteine + methyl benzoate [RN:R10447]
Reaction(KEGG)
Substrate
S-adenosyl-L-methionine [CPD:C00019];
benzoate [CPD:C00180]
Product
S-adenosyl-L-homocysteine [CPD:C00021];
methyl benzoate [CPD:C20645]
Comment
While the enzyme from the plant Zea mays is specific for benzoate [6], the enzymes from Arabidopsis species and Clarkia breweri also catalyse the reaction of EC 2.1.1.274, salicylate 1-O-methyltransferase [1,5]. In snapdragon (Antirrhinum majus) two isoforms are found, one specific for benzoate [2,3] and one that is also active towards salicylate [4]. The volatile product is an important scent compound in some flowering species [2].
History
EC 2.1.1.273 created 2013
Orthology
K21482  benzoate O-methyltransferase
K21484  benzoate/salicylate 1-O-methyltransferase
Genes
ATH: AT3G11480(BSMT1) AT5G04370(NAMT1) AT5G04380 AT5G66430
ALY: ARALYDRAFT_487217 ARALYDRAFT_897350
CRB: 17893670
CSAT: 104708682 104727399 104734448 104745350 104745353 104745842 104746543 104762932 104764901 104766009 104768626 104773442 109130817
EUS: EUTSA_v10013754mg EUTSA_v10022292mg
BRP: 103837152 103847295 103847297 103847298 103847299 103855566 103859391 103870342 103870344
BNA: 106345178 106345495 106346584 106353051 106362614 106364005 106366900 106370700 106372697 106372698 106383478 106416291 106416341 106423490 106436478 106436480 106436482 106440340 106442990
BOE: 106302931 106313641 106316499 106318326 106318327 106329214 106332554
THJ: 104819197 104819198 104820147
CPAP: 110826209
TCC: 18589945
GRA: 105775995
DZI: 111309877
POP: 7487202
JRE: 108983849
SPEN: 107015380
CANN: 107857182
NSY: 104246528
NTO: 104120721
LSV: 111908135
CCAV: 112504667
DCR: 108203055
NNU: 104595931
OBR: 102706569
SBI: 110434364
SITA: 101766563
 » show all
Taxonomy
Reference
1  [PMID:10375393]
  Authors
Ross JR, Nam KH, D'Auria JC, Pichersky E
  Title
S-Adenosyl-L-methionine:salicylic acid carboxyl methyltransferase, an enzyme involved in floral scent production and plant defense, represents a new class of  plant methyltransferases.
  Journal
Arch Biochem Biophys 367:9-16 (1999)
DOI:10.1006/abbi.1999.1255
Reference
2  [PMID:10852939]
  Authors
Dudareva N, Murfitt LM, Mann CJ, Gorenstein N, Kolosova N, Kish CM, Bonham C, Wood K
  Title
Developmental regulation of methyl benzoate biosynthesis and emission in snapdragon flowers.
  Journal
Plant Cell 12:949-61 (2000)
DOI:10.1105/tpc.12.6.949
  Sequence
Reference
3  [PMID:11051108]
  Authors
Murfitt LM, Kolosova N, Mann CJ, Dudareva N
  Title
Purification and characterization of S-adenosyl-L-methionine:benzoic acid carboxyl methyltransferase, the enzyme responsible for biosynthesis of the volatile ester methyl benzoate in flowers of Antirrhinum majus.
  Journal
Arch Biochem Biophys 382:145-51 (2000)
DOI:10.1006/abbi.2000.2008
Reference
4  [PMID:12361714]
  Authors
Negre F, Kolosova N, Knoll J, Kish CM, Dudareva N
  Title
Novel S-adenosyl-L-methionine:salicylic acid carboxyl methyltransferase, an enzyme responsible for biosynthesis of methyl salicylate and methyl benzoate, is  not involved in floral scent production in snapdragon flowers.
  Journal
Arch Biochem Biophys 406:261-70 (2002)
DOI:10.1016/S0003-9861(02)00458-7
Reference
5  [PMID:14617060]
  Authors
Chen F, D'Auria JC, Tholl D, Ross JR, Gershenzon J, Noel JP, Pichersky E
  Title
An Arabidopsis thaliana gene for methylsalicylate biosynthesis, identified by a biochemical genomics approach, has a role in defense.
  Journal
Plant J 36:577-88 (2003)
DOI:10.1046/j.1365-313X.2003.01902.x
  Sequence
[ath:AT3G11480]
Reference
6  [PMID:20519632]
  Authors
Kollner TG, Lenk C, Zhao N, Seidl-Adams I, Gershenzon J, Chen F, Degenhardt J
  Title
Herbivore-induced SABATH methyltransferases of maize that methylate anthranilic acid using s-adenosyl-L-methionine.
  Journal
Plant Physiol 153:1795-807 (2010)
DOI:10.1104/pp.110.158360
  Sequence
[zma:113604963]
Other DBs
ExplorEnz - The Enzyme Database: 2.1.1.273
IUBMB Enzyme Nomenclature: 2.1.1.273
ExPASy - ENZYME nomenclature database: 2.1.1.273
BRENDA, the Enzyme Database: 2.1.1.273

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