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Literature summary for 2.1.1.273 extracted from

  • Kolosova, N.; Sherman, D.; Karlson, D.; Dudareva, N.
    Cellular and subcellular localization of S-adenosyl-L-methionine:benzoic acid carboxyl methyltransferase, the enzyme responsible for biosynthesis of the volatile ester methylbenzoate in snapdragon flowers (2001), Plant Physiol., 126, 956-964.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.273

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Antirrhinum majus 5829
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + benzoate Antirrhinum majus
-
 S-adenosyl-L-homocysteine + methyl benzoate
-
 ?

Organism

Organism UniProt Comment Textmining
Antirrhinum majus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
epidermis the enzyme is localized predominantly in the conical cells of the inner epidermal layer and, to a much lesser extent, in the cells of the outer epidermis of flower petal lobes. The enzyme is also located in the inner epidermis of the corolla tube with little protein detected in the outer epidermis and in the yellow hairs within the tube on the bee’s way to the nectar Antirrhinum majus
-
flower
-
 Antirrhinum majus
-
petal
-
 Antirrhinum majus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + benzoate
-
 Antirrhinum majus S-adenosyl-L-homocysteine + methyl benzoate
-
 ?

Synonyms

Synonyms Comment Organism
BAMT
-
 Antirrhinum majus
S-adenosyl-L-methionine:benzoic acid carboxyl methyltransferase
-
 Antirrhinum majus

General Information

General Information Comment Organism
physiological function the enzyme is responsible for biosynthesis of the volatile ester methylbenzoate in snapdragon flowers Antirrhinum majus