2.7.1.190: aminoglycoside 2''-phosphotransferase
This is an abbreviated version!
For detailed information about aminoglycoside 2''-phosphotransferase, go to the full flat file.
Word Map on EC 2.7.1.190
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2.7.1.190
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aph3\'-iiia
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kanamycin
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enterococci
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aac6\'-ie-aph2\'\'-ia
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faecium
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aminoglycoside-modifying
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phosphotransferases
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aph2\'\'-ic
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amikacin
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gentamicin-resistant
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aac6\'-aph2
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tobramycin
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4,6-disubstituted
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casseliflavus
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aac6'-ie
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ant6\'-ia
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gallinarum
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aminoglycoside-resistance
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lividomycin
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butirosin
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o-phosphorylation
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sisomicin
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durans
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molecular biology
- 2.7.1.190
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aph3\'-iiia
- kanamycin
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enterococci
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aac6\'-ie-aph2\'\'-ia
- faecium
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aminoglycoside-modifying
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phosphotransferases
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aph2\'\'-ic
- amikacin
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gentamicin-resistant
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aac6\'-aph2
- tobramycin
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4,6-disubstituted
- casseliflavus
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aac6'-ie
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ant6\'-ia
- gallinarum
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aminoglycoside-resistance
- lividomycin
- butirosin
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o-phosphorylation
- sisomicin
- durans
- molecular biology
Reaction
Synonyms
AAC(6')-APH(2''), AAC(6')-Ie/APH(2'')-Ia, aac6-aph2, aacA-aphD, AME, aminoglycoside (2'') kinase, aminoglycoside 2''-phosphotransferase IVa, aminoglycoside 2''-phosphotransferase type IIIa, aminoglycoside kinase, aminoglycoside phosphotransferase, aminoglycoside-2''-phosphotransferase, aminoglycoside-2''-phosphotransferase type IVa, aminoglycoside-modification enzyme, APH, APH(2''), APH(2'')-Ia, APH(2'')-Ia aminoglycoside resistance enzyme, APH(2'')-Id, Aph(2'')-If, APH(2'')-IIIa, APH(2'')-IVa, aphD, AphSR2, bifunctional 6'-aminoglycoside acetyltransferase/2"-aminoglycoside phosphotransferase, bifunctional AAC/APH, bifunctional aminoglycoside acetyltransferase(6')-Ie/aminoglycoside phosphotransferase(2'')-Ia, bifunctional aminoglycoside acetyltransferase/phosphotransferase, gentamicin kinase, gentamicin phosphotransferase, gentamicin resistance protein
ECTree
2.7.1.190 aminoglycoside 2''-phosphotransferaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 2.7.1.190 - aminoglycoside 2''-phosphotransferase
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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
ATP + gentamicin
ADP + gentamicin 2''-phosphate
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GTP is preferred over ATP
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?
GTP + gentamicin C
GDP + gentamicin C 2''-phosphate
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GTP is preferred over ATP
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?
GTP + gentamicin C
GDP + gentamicin C 2''-phosphate
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GTP is preferred over ATP
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?
GTP + kanamycin A
GDP + kanamycin A 2''-phosphate
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?
GTP + lividomycin
GDP + lividomycin 2''-phosphate
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enzyme binding structure analysis, overview
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additional information
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no substrates: 4,5-disubstituted antibiotics and the atypical aminoglycoside neamine
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additional information
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no substrates: 4,5-disubstituted antibiotics and the atypical aminoglycoside neamine
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?
additional information
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enzyme assay with coupling the release of ADP to a pyruvate kinase/lactate dehydrogenase reaction
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additional information
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most aminoglycosides are based upon a neamine core, i.e. a central 2-deoxystreptamine (2-DOS) ring with an aminohexose sugar linked to 2-DOS at the 4-position. These rings form the minimal active element of an aminoglycoside antibiotic, and two subclasses of aminoglycosides are formed from elaboration of this scaffold. Addition of rings to the 5- and 6-positions of 2-DOS differentiate aminoglycosides into the 4,5-disubstituted (ribostamycin, neomycin, and lividomycin) and 4,6-disusbstituted (kanamycin, gentamicin, and dibekacin) groups
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additional information
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random sequential Bi Bi mechanism. At pH 7.5 the release of guanosine triphosphate is rate-limiting. No substrates: amikacin, isepamicin, neomycin, butirosin, lividomycin A , paromomycin, spectinomycin, streptomycin, apramycin, hygromycin, neamine
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?
additional information
?
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substrate binding in the APH(2'') enzymes, overview. The substrate molecules are bound in essentially the same orientation in all structures. The neamine moiety of aminoglycosides is nestled against the core subdomain and helix alpha9 such that the A ring projects towards motif 3 in the helical subdomain and the B ring points towards motif 1 and motif 2 in the core subdomain. The C ring then projects back towards the helical domain
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additional information
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GTP is the exclusive phosphate donor at intracellular nucleotide levels
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additional information
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the bifunctional enzyme AAC(6')-APH(2'') enzyme shows acetyltransferase activity and phosphotransferase activity, activity measurement in a sigle assay. GTP is more qualified as a phosphate donor than ATP to cause phosphorylation events of AAC(6')-APH(2'')
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