Isobutyraldoxime O-methyltransferase

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isobutyraldoxime O-methyltransferase
Identifiers
EC no. 2.1.1.91
CAS no. 95471-32-2
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BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
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In enzymology, an isobutyraldoxime O-methyltransferase (EC 2.1.1.91) is an enzyme that catalyzes the chemical reaction

S-adenosyl-L-methionine + 2-methylpropanal oxime S-adenosyl-L-homocysteine + 2-methylpropanal O-methyloxime

Thus, the two substrates of this enzyme are S-adenosyl methionine and 2-methylpropanal oxime, whereas its two products are S-adenosylhomocysteine and 2-methylpropanal O-methyloxime.

This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:2-methylpropanal-oxime O-methyltransferase. Other names in common use include aldoxime methyltransferase, S-adenosylmethionine:aldoxime O-methyltransferase, and aldoxime O-methyltransferase.

Related Research Articles

<i>S</i>-Adenosyl methionine Chemical compound found in all domains of life with largely unexplored effects

S-Adenosyl methionine (SAM), also known under the commercial names of SAMe, SAM-e, or AdoMet, is a common cosubstrate involved in methyl group transfers, transsulfuration, and aminopropylation. Although these anabolic reactions occur throughout the body, most SAM is produced and consumed in the liver. More than 40 methyl transfers from SAM are known, to various substrates such as nucleic acids, proteins, lipids and secondary metabolites. It is made from adenosine triphosphate (ATP) and methionine by methionine adenosyltransferase. SAM was first discovered by Giulio Cantoni in 1952.

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In enzymology, an inositol 3-methyltransferase is an enzyme that catalyzes the chemical reaction

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<span class="mw-page-title-main">Magnesium protoporphyrin IX methyltransferase</span>

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<span class="mw-page-title-main">Protein-glutamate O-methyltransferase</span>

In enzymology, a protein-glutamate O-methyltransferase is an enzyme that catalyzes the chemical reaction

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<span class="mw-page-title-main">Uroporphyrinogen-III C-methyltransferase</span> Class of enzymes

Uroporphyrinogen-III C-methyltransferase, uroporphyrinogen methyltransferase, uroporphyrinogen-III methyltransferase, adenosylmethionine-uroporphyrinogen III methyltransferase, S-adenosyl-L-methionine-dependent uroporphyrinogen III methylase, uroporphyrinogen-III methylase, SirA, CysG, CobA, uroporphyrin-III C-methyltransferase, S-adenosyl-L-methionine:uroporphyrin-III C-methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:uroporphyrinogen-III C-methyltransferase. This enzyme catalyses the following chemical reaction

References


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