Enzyme

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     2. Transferases
        2.4 Glycosyltransferases
            2.4.1 Hexosyltransferases
ID:2.4.1.187
Description:mannosaminyltransferase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.4.1.187
BRENDA Enzyme Link: BRENDA 2.4.1.187
KEGG Enzyme Link: KEGG2.4.1.187
BioCyc Enzyme Link: BioCyc 2.4.1.187
ExPASy Enzyme Link: ExPASy2.4.1.187
EC2PDB Enzyme Link: EC2PDB 2.4.1.187
ExplorEnz Enzyme Link: ExplorEnz 2.4.1.187
PRIAM enzyme-specific profiles Link: PRIAM 2.4.1.187
IntEnz Enzyme Link: IntEnz 2.4.1.187
MEDLINE Enzyme Link: MEDLINE 2.4.1.187
MSA:

2.4.1.187;

Phylogenetic Tree:

2.4.1.187;

Uniprot:
M-CSA:
RHEA:16053 N-acetyl-alpha-D-glucosaminyl-1-diphospho-di-trans,octa-cis-undecaprenol + UDP-N-acetyl-alpha-D-mannosamine = H(+) + N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate + UDP
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[O;H0;+0:4]-[*:5].[*:6]-[OH;+0:7]>>[*:1]-[CH;+0:2](-[*:3])-[O;H0;+0:7]-[*:6].[*:5]-[OH;+0:4]
Reaction
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References

TitleAuthorsDatePubMed ID
Partial purification and properties of UDP-N-acetylmannosamine:N-acetylglucosaminyl pyrophosphorylundecaprenol N-acetylmannosaminyltransferase from Bacillus subtilis.Murazumi N, Kumita K, Araki Y, Ito E1988 Dec2977387
In vitro reconstitution of two essential steps in wall teichoic acid biosynthesis.Ginsberg C, Zhang YH, Yuan Y, Walker S2006 Feb 1717163636
Acceptor substrate selectivity and kinetic mechanism of Bacillus subtilis TagA.Zhang YH, Ginsberg C, Yuan Y, Walker S2006 Sep 1216953575
A revised pathway proposed for Staphylococcus aureus wall teichoic acid biosynthesis based on in vitro reconstitution of the intracellular steps.Brown S, Zhang YH, Walker S2008 Jan18215769