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Enzyme Nomenclature
Information on EC 2.3.1.59 - gentamicin 2'-N-acetyltransferase
Word Map on EC 2.3.1.59
- 2.3.1.59
- stuartii
-
providencia
-
aminoglycoside
- peptidoglycan
-
aac2\'-ia
- beta-galactosidase
-
o-acetylation
- tobramycin
-
proteeae
- tetracycline
-
spent
-
proteus
-
autolytic
- netilmicin
-
coccobacilli
-
mid-exponential
-
formers
-
density-dependent
- analysis
- ubiquinone
-
irregular
- chloramphenicol
-
2\'-amino
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.3.1.59
-
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RECOMMENDED NAME
GeneOntology No.
gentamicin 2'-N-acetyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + gentamicin C1a = CoA + N2'-acetylgentamicin C1a
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
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-
-
-
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:gentamicin-C1a N2'-acetyltransferase
The antibiotics gentamicin A, sisomicin, tobramycin, paromomycin, neomycin B, kanamycin B and kanamycin C can also act as acceptors.
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CAS REGISTRY NUMBER
COMMENTARY
50864-40-9
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + butirosin
CoA + ?
-
acetylated at 30% the rate of gentamicin C1
-
-
?
acetyl-CoA + dideoxykanamycin
CoA + N2'-diacetyldideoxykanamycin
-
acetylated at 92% the rate of gentamicin C1
-
-
?
acetyl-CoA + gentamicin B
CoA + N2'-acetylgentamycin
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7% of the activity with gentamicin C1
-
-
?
acetyl-CoA + neomycin B
CoA + N2'-acetylneomycin
-
acetylated at 10% the rate of gentamicin C1
-
-
?
acetyl-CoA + ribostamycin
CoA + N2'-acetylribostamycin
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acetylated at 15% the rate of gentamicin C1
-
-
?
acetyl-CoA + gentamicin C1
CoA + N2'-acetylgentamicin C1
-
best substrate
-
-
?
acetyl-CoA + gentamicin C1
CoA + N2'-acetylgentamicin C1
-
best substrate
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N2'-acetylgentamicin C1a
-
acetylated at 86% the rate of gentamicin C1
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N2'-acetylgentamicin C1a
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acetylated at 86% the rate of gentamicin C1
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N2'-acetylgentamicin C1a
-
-
-
-
?
acetyl-CoA + gentamicin C1a
CoA + N2'-acetylgentamicin C1a
-
acetylates 2'-amino group of hexose moiety
-
?
acetyl-CoA + kanamycin B
CoA + N2-acetylkanamycin B
-
acetylated at 14% the rate of gentamicin C1
-
-
?
acetyl-CoA + kanamycin C
CoA + N2'-acetylkanamycin C
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acetylated at 40% the rate of gentamicin C1
-
-
?
acetyl-CoA + sisomicin
CoA + N3'-acetylsisomicin
-
acetylated at 71% the rate of gentamicin C1
-
-
-
acetyl-CoA + sisomicin
CoA + N3'-acetylsisomicin
-
acetylated at 71% the rate of gentamicin C1
-
-
-
acetyl-CoA + tobramycin
CoA + N2'-acetyltobramycin
-
acetylated at 58% the rate of gentamicin C1
-
-
?
acetyl-CoA + tobramycin
CoA + N2'-acetyltobramycin
-
acetylated at 58% the rate of gentamicin C1
-
-
?
acetyl-CoA of soluble fragments of peptidoglycan + tobramycin
?
-
acetylated at 58% the rate of gentamicin C1
-
-
?
acetyl-CoA of soluble fragments of peptidoglycan + tobramycin
?
-
-
-
-
?
N-acetyl-D-glucosamine + tobramycin
D-glucosamine + N2'-acetyltobramycin
-
acetylated at 58% the rate of gentamicin C1
-
-
?
N-acetyl-D-glucosamine + tobramycin
D-glucosamine + N2'-acetyltobramycin
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-
-
-
?
additional information
?
-
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no substrates are kanamycin A and 1-hydroxyaminobutyric acid kanamycin A-derivative BB-K 8
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-
-
additional information
?
-
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no substrates are kanamycin A and 1-hydroxyaminobutyric acid kanamycin A-derivative BB-K 8
-
-
-
additional information
?
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the enzyme may contribute to the O-acetylation of peptidoglycan
-
-
?
additional information
?
-
-
enzyme may have a physiological role in secondary metabolism, its activity on aminoglycosides is simply fortouitous
-
-
?
additional information
?
-
-
the enzyme contributes to the O-acetylation of peptidoglycan. Mutants that either underexpress or overexpress the aac(2')-Ia gene are characterized phenotypically to possess either lower or higher levels of peptidoglycan O-acetylation, respectively, compared to the wild-type. Providencia stuartii PR100, with 42-44% peptidoglycan O-acetylation compared to 54% of the wild-type, appears as irregular rods. Strains PR50.LM3 and PR51, with increased levels of peptidoglycan O-acetylation, 63% and 65% respectively, appear as coccobacilli or chain formers
-
-
?
additional information
?
-
-
the enzyme may contribute to the O-acetylation of peptidoglycan
-
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the enzyme may contribute to the O-acetylation of peptidoglycan
-
-
?
additional information
?
-
-
enzyme may have a physiological role in secondary metabolism, its activity on aminoglycosides is simply fortouitous
-
-
?
additional information
?
-
-
the enzyme contributes to the O-acetylation of peptidoglycan. Mutants that either underexpress or overexpress the aac(2')-Ia gene are characterized phenotypically to possess either lower or higher levels of peptidoglycan O-acetylation, respectively, compared to the wild-type. Providencia stuartii PR100, with 42-44% peptidoglycan O-acetylation compared to 54% of the wild-type, appears as irregular rods. Strains PR50.LM3 and PR51, with increased levels of peptidoglycan O-acetylation, 63% and 65% respectively, appear as coccobacilli or chain formers
-
-
?
additional information
?
-
-
the enzyme may contribute to the O-acetylation of peptidoglycan
-
-
?
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
activity in crude enzyme preparation is stable to repeated freezing and thawing
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
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LINKS TO OTHER DATABASES (specific for EC-Number 2.3.1.59)
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