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
Butirosin and neomycin biosynthesis
Biosynthesis of secondary metabolites
Orthology
K13551  
2'-N-acetylparomamine deacetylase
K17078  
2'-N-acetylparomamine deacetylase / 2'''-acetyl-6'''-hydroxyneomycin deacetylase
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 (2007) 1462-4.
  Sequence
[up:Q4H4F3]
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 (2008) 865-9.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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