KEGG   ENZYME: 3.5.1.112Help
Entry
EC 3.5.1.112                Enzyme                                 

Name
2'-N-acetylparomamine deacetylase;
btrD (gene name);
neoL (gene name);
kanN (gene name)
Class
Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In linear amides
BRITE hierarchy
Sysname
2'-N-acetylparomamine hydrolase (acetate-forming)
Reaction(IUBMB)
2'-N-acetylparomamine + H2O = paromamine + acetate [RN:R08895]
Reaction(KEGG)
Substrate
2'-N-acetylparomamine [CPD:C17582];
H2O [CPD:C00001]
Product
paromamine [CPD:C01743];
acetate [CPD:C00033]
Comment
Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin. The enzyme from the bacterium Streptomyces fradiae can also accept 2'''-acetyl-6'''-hydroxyneomycin C as substrate, cf. EC 3.5.1.113, 2'''-acetyl-6'''-hydroxyneomycin C deacetylase [2].
History
EC 3.5.1.112 created 2012
Pathway
ec00524  Neomycin, kanamycin and gentamicin biosynthesis
ec01130  Biosynthesis of antibiotics
Orthology
K13551  2'-N-acetylparomamine deacetylase
K17078  2'-N-acetylparomamine deacetylase / 2'''-acetyl-6'''-hydroxyneomycin deacetylase
Genes
SRN: A4G23_05119(neoL)
Taxonomy
Reference
1  [PMID:17226887]
  Authors
Truman AW, Huang F, Llewellyn NM, Spencer JB.
  Title
Characterization of the enzyme BtrD from Bacillus circulans and revision of its functional assignment in the biosynthesis of butirosin.
  Journal
Angew Chem Int Ed Engl 46:1462-4 (2007)
DOI:10.1002/anie.200604194
Reference
2  [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 9:865-9 (2008)
DOI:10.1002/cbic.200700717
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 3.5.1.112
IUBMB Enzyme Nomenclature: 3.5.1.112
ExPASy - ENZYME nomenclature database: 3.5.1.112
BRENDA, the Enzyme Database: 3.5.1.112

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