Information on EC 3.5.1.112 - 2'-N-acetylparomamine deacetylase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
3.5.1.112
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RECOMMENDED NAME
GeneOntology No.
2'-N-acetylparomamine deacetylase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2'-N-acetylparomamine + H2O = paromamine + acetate
show the reaction diagram
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PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
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Butirosin and neomycin biosynthesis
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kanamycin biosynthesis
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paromamine biosynthesis I
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paromamine biosynthesis II
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SYSTEMATIC NAME
IUBMB Comments
2'-N-acetylparomamine hydrolase (acetate-forming)
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].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
btrD
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gene name
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kanN
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gene name
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neoL
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gene name
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ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
BtrD functions as a deacetylase in the formation of butirosin
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N-acetylparomamine + H2O
paromamine + acetate
show the reaction diagram
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-
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?
2'-N-acetylparomamine + H2O
paromamine + acetate
show the reaction diagram
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?
additional information
?
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enzyme shows no activity towards neamine, ribostamycin, and butirosin
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pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
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assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
28
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assay at
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
purified with TALON cobalt affinity resin
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Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli BL21(DE3) as an N-terminally His6-tagged protein
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expressed as a His-tagged fusion protein in Escherichia coli
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