KEGG   ENZYME: 2.1.1.301
Entry
EC 2.1.1.301                Enzyme                                 
Name
cypemycin N-terminal methyltransferase;
CypM
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
Sysname
S-adenosyl-L-methionine:N-terminal L-alanine-[cypemycin] N-methyltransferase
Reaction(IUBMB)
2 S-adenosyl-L-methionine + N-terminal L-alanine-[cypemycin] = 2 S-adenosyl-L-homocysteine + N-terminal N,N-dimethyl-L-alanine-[cypemycin]
Substrate
S-adenosyl-L-methionine [CPD:C00019];
N-terminal L-alanine-[cypemycin]
Product
S-adenosyl-L-homocysteine [CPD:C00021];
N-terminal N,N-dimethyl-L-alanine-[cypemycin]
Comment
The enzyme, isolated from the bacterium Streptomyces sp. OH-4156, can methylate a variety of linear oligopeptides, cyclic peptides such as nisin and haloduracin, and the epsilon-amino group of lysine [2]. Cypemycin is a peptide antibiotic, a member of the linaridins, a class of posttranslationally modified ribosomally synthesized peptides.
History
EC 2.1.1.301 created 2014
Orthology
K21459  cypemycin N-terminal methyltransferase
Genes
ATYA9R16_008560
SGRSGR_6362
SGOBtest1122_04255
Reference
1  [PMID:20805503]
  Authors
Claesen J, Bibb M
  Title
Genome mining and genetic analysis of cypemycin biosynthesis reveal an unusual class of posttranslationally modified peptides.
  Journal
Proc Natl Acad Sci U S A 107:16297-302 (2010)
DOI:10.1073/pnas.1008608107
  Sequence
Reference
2  [PMID:22841713]
  Authors
Zhang Q, van der Donk WA
  Title
Catalytic promiscuity of a bacterial alpha-N-methyltransferase.
  Journal
FEBS Lett 586:3391-7 (2012)
DOI:10.1016/j.febslet.2012.07.050
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 2.1.1.301
IUBMB Enzyme Nomenclature: 2.1.1.301
ExPASy - ENZYME nomenclature database: 2.1.1.301
BRENDA, the Enzyme Database: 2.1.1.301
LinkDB

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