Entry
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
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
ec00524 Neomycin, kanamycin and gentamicin biosynthesis
ec01110 Biosynthesis of secondary metabolites
Orthology
K13550 2-deoxystreptamine N-acetyl-D-glucosaminyltransferase / 2-deoxystreptamine glucosyltransferase
Genes
Taxonomy
Reference
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
Sequence
Reference
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
Sequence
Other DBs
ExPASy - ENZYME nomenclature database: 2.4.1.283