KEGG   ENZYME: 2.1.1.235Help
Entry
EC 2.1.1.235                Enzyme                                 

Name
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose N,N-dimethyltransferase;
TylM1
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
BRITE hierarchy
Sysname
S-adenosyl-L-methionine:dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose 3-N,N-dimethyltransferase
Reaction(IUBMB)
2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose = 2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-glucopyranose [RN:R06439]
Reaction(KEGG)
Substrate
S-adenosyl-L-methionine [CPD:C00019];
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
Product
S-adenosyl-L-homocysteine [CPD:C00021];
dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-glucopyranose
Comment
The enzyme is involved in the biosynthesis of mycaminose, an essential structural component of the macrolide antibiotic tylosin, which is produced by the bacterium Streptomyces fradiae.
History
EC 2.1.1.235 created 2011
Pathway
ec00523  Polyketide sugar unit biosynthesis
ec01130  Biosynthesis of antibiotics
Orthology
K13307  dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose N,N-dimethyltransferase
Genes
SAMB: SAM23877_5630(srm7)
MAU: Micau_3984
MIL: ML5_4437
Taxonomy
Reference
1  [PMID:12119032]
  Authors
Chen H, Yamase H, Murakami K, Chang CW, Zhao L, Zhao Z, Liu HW
  Title
Expression, purification, and characterization of two N,N-dimethyltransferases, tylM1 and desVI, involved in the biosynthesis of mycaminose and desosamine.
  Journal
Biochemistry 41:9165-83 (2002)
DOI:10.1021/bi020245j
  Sequence
Reference
2  [PMID:21142177]
  Authors
Carney AE, Holden HM
  Title
Molecular architecture of TylM1 from Streptomyces fradiae: an N,N-dimethyltransferase involved in the production of dTDP-D-mycaminose.
  Journal
Biochemistry 50:780-7 (2011)
DOI:10.1021/bi101733y
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 2.1.1.235
IUBMB Enzyme Nomenclature: 2.1.1.235
ExPASy - ENZYME nomenclature database: 2.1.1.235
BRENDA, the Enzyme Database: 2.1.1.235

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