KEGG ENZYME: 2.1.1.402

ENZYME: 2.1.1.402

Entry

EC 2.1.1.402                Enzyme

Name

sialate 8-O-methyltransferase;
N-acetylneuraminate 8-O-methyltransferase

Class

Transferases;
Transferring one-carbon groups;
Methyltransferases

Sysname

S-adenosyl-L-methionine:sialate-8-O-methyltransferase

Reaction(IUBMB)

S-adenosyl-L-methionine + N-acetylneuraminate = S-adenosyl-L-homocysteine + N-acetyl-8-O-methyl-neuraminate [RN:R13501]

Reaction(KEGG)

R13501

Substrate

S-adenosyl-L-methionine [CPD:C00019];
N-acetylneuraminate [CPD:C00270]

Product

S-adenosyl-L-homocysteine [CPD:C00021];
N-acetyl-8-O-methyl-neuraminate [CPD:C23040]

Comment

The enzyme has been isolated from gonads of the starfish Asterias rubens. It methylates N-glycolylneuraminate with equal specificity. Oligosaccharides containing N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-D-galactosyl structures are also methylated.

History

EC 2.1.1.402 created 2025

Reference

1 [PMID:1576206]

Authors

Bergwerff AA, Hulleman SH, Kamerling JP, Vliegenthart JF, Shaw L, Reuter G, Schauer R.

Title

Nature and biosynthesis of sialic acids in the starfish Asterias rubens. Identification of sialo-oligomers and detection of S-adenosyl-L-methionine: N-acylneuraminate 8-O-methyltransferase and CMP-N-acetylneuraminate monooxygenase activities.

Journal

Biochimie 74:25-37 (1992)
DOI:10.1016/0300-9084(92)90181-d

Reference

2 [PMID:9490063]

Authors

Kelm A, Shaw L, Schauer R, Reuter G.

Title

The biosynthesis of 8-O-methylated sialic acids in the starfish Asterias rubens--isolation and characterisation of S-adenosyl-L-methionine:sialate-8-O-methyltransferase.

Journal

Eur J Biochem 251:874-84 (1998)
DOI:10.1046/j.1432-1327.1998.2510874.x

Other DBs

ExplorEnz - The Enzyme Database:

2.1.1.402

IUBMB Enzyme Nomenclature:

2.1.1.402

ExPASy - ENZYME nomenclature database:

2.1.1.402

BRENDA, the Enzyme Database:

2.1.1.402

LinkDB

DBGET integrated database retrieval system