KEGG   ENZYME: 2.4.1.283Help
Entry
EC 2.4.1.283                Enzyme                                 

Name
2-deoxystreptamine N-acetyl-D-glucosaminyltransferase;
btrM (gene name);
neoD (gene name);
kanF (gene name)
Class
Transferases;
Glycosyltransferases;
Hexosyltransferases
BRITE hierarchy
Sysname
UDP-N-acetyl-alpha-D-glucosamine:2-deoxystreptamine N-acetyl-D-glucosaminyltransferase
Reaction(IUBMB)
UDP-N-acetyl-alpha-D-glucosamine + 2-deoxystreptamine = UDP + 2'-N-acetylparomamine [RN:R08894]
Reaction(KEGG)
Substrate
UDP-N-acetyl-alpha-D-glucosamine [CPD:C00043];
2-deoxystreptamine [CPD:C02627]
Product
UDP [CPD:C00015];
2'-N-acetylparomamine [CPD:C17582]
Comment
Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin. Unlike the enzyme from the bacterium Streptomyces kanamyceticus, which can also accept UDP-D-glucose [2] (cf. EC 2.4.1.284, 2-deoxystreptamine glucosyltransferase), the enzyme from Bacillus circulans can only accept UDP-N-acetyl-alpha-D-glucosamine [1].
History
EC 2.4.1.283 created 2012
Pathway
Neomycin, kanamycin and gentamicin biosynthesis
Biosynthesis of antibiotics
Orthology
K13550  
2-deoxystreptamine N-acetyl-D-glucosaminyltransferase / 2-deoxystreptamine glucosyltransferase
Reference
1  [PMID:18311744]
  Authors
Yokoyama K, Yamamoto Y, Kudo F, Eguchi T.
  Title
Involvement of two distinct N-acetylglucosaminyltransferases and a dual-function  deacetylase in neomycin biosynthesis.
  Journal
Chembiochem. 9 (2008) 865-9.
  Sequence
Reference
2  [PMID:21983602]
  Authors
Park JW, Park SR, Nepal KK, Han AR, Ban YH, Yoo YJ, Kim EJ, Kim EM, Kim D, Sohng JK, Yoon YJ
  Title
Discovery of parallel pathways of kanamycin biosynthesis allows antibiotic manipulation.
  Journal
Nat. Chem. Biol. 7 (2011) 843-52.
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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