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Information on EC 2.1.1.142 - cycloartenol 24-C-methyltransferase and Organism(s) Pneumocystis carinii and UniProt Accession Q96WX4

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EC Tree
     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.142 cycloartenol 24-C-methyltransferase
IUBMB Comments
S-Adenosyl-L-methionine methylates the Si face of the 24(25)-double bond with elimination of a hydrogen atom from the pro-Z methyl group at C-25.
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Pneumocystis carinii
UNIPROT: Q96WX4
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Word Map
The taxonomic range for the selected organisms is: Pneumocystis carinii
The enzyme appears in selected viruses and cellular organisms
Synonyms
24-smt, sterol methyltransferase, sterol methyl transferase, sterol c24-methyltransferase, sam:smt, sterol c-24 methyltransferase, ghsmt2-1, ghsmt2-2, sterol methyltransferase2, smt2-1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(S)-adenosyl-L-methionine-DELTA24-sterol methyltransferase
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(S)-adenosyl-L-methionine:DELTA24(25)-sterol methyltransferase
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DELTA24(25)-sterol methyltransferase
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DELTA24-sterol methyltransferase
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SAM-DELTA24 sterol transmethylase
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sterol C-methyltransferase
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zymosterol-24-methyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
transfer of methyl group
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:cycloartenol 24-C-methyltransferase
S-Adenosyl-L-methionine methylates the Si face of the 24(25)-double bond with elimination of a hydrogen atom from the pro-Z methyl group at C-25.
CAS REGISTRY NUMBER
COMMENTARY hide
37257-07-1
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + lanosterol
S-adenosyl-L-homocysteine + 24(28)-methylene-24,25-dihydro-lanosterol
show the reaction diagram
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme catalyzes both the reactions of EC 2.1.1.41 and EC 2.1.1.142
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
enzyme transfers either one or two methyl groups to the C-24 position of the sterol side chain producing both C28 and C29 24-alkylsterols in approximately the same proportions. Expression of SAM:SMT in a Saccharomyces cerevisiae Erg6 mutant restores its ability to produce ergosterol as the major sterol, and also results in low levels of C29 sterols such as pneumocysterol
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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x * 43000, SDS-PAGE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kaneshiro, E.; Johnston, L.; Nkinin, S.; Romero, B.; Giner, J.
Sterols of Saccharomyces cerevisiae erg6 knockout mutant expressing the Pneumocystis carinii S-adenosylmethionine sterol C-24 methyltransferase (SAM SMT)
J. Eukaryot. Microbiol.
62
298-306
2015
Pneumocystis carinii (Q96WX4), Pneumocystis carinii, Pneumocystis carinii B80 (Q96WX4)
Manually annotated by BRENDA team