EC number:2.1.1.301

Enzyme

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     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.301
Description:Cypemycin N-terminal methyltransferase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.301
BRENDA Enzyme Link: BRENDA 2.1.1.301
KEGG Enzyme Link: KEGG2.1.1.301
BioCyc Enzyme Link: BioCyc 2.1.1.301
ExPASy Enzyme Link: ExPASy2.1.1.301
EC2PDB Enzyme Link: EC2PDB 2.1.1.301
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.301
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.301
IntEnz Enzyme Link: IntEnz 2.1.1.301
MEDLINE Enzyme Link: MEDLINE 2.1.1.301

EC number:2.1.1.301

MSA:

2.1.1.301;
Phylogenetic Tree:

2.1.1.301;
Uniprot:
M-CSA:
RHEA:14393 N-terminal L-alanyl-[cypemycin] + 2 S-adenosyl-L-methionine = 3 H(+) + N-terminal N,N-dimethyl-L-alanyl-[cypemycin] + 2 S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[NH2;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6].[*:7]-[S+;H0:8](-[*:9])-[CH3;+0:10]>>[*:1]-[N;H0;+0:2](-[CH3;+0:10])-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5].[*:7]-[S;H0;+0:8]-[*:9]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Catalytic promiscuity of a bacterial α-N-methyltransferase.Zhang Q, van der Donk WA2012 Sep 2122841713
Genome mining and genetic analysis of cypemycin biosynthesis reveal an unusual class of posttranslationally modified peptides.Claesen J, Bibb M2010 Sep 1420805503