EC number:2.7.1.95

Enzyme

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     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.1 Phosphotransferases with an alcohol group as acceptor
ID:2.7.1.95
Description:Kanamycin kinase.
Alternative Name: Neomycin-kanamycin phosphotransferase.
APH(3').
Aminoglycoside 3'-phosphotransferase.
Cath: 3.30.200.20; 3.90.1200.10;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.1.95
BRENDA Enzyme Link: BRENDA 2.7.1.95
KEGG Enzyme Link: KEGG2.7.1.95
BioCyc Enzyme Link: BioCyc 2.7.1.95
ExPASy Enzyme Link: ExPASy2.7.1.95
EC2PDB Enzyme Link: EC2PDB 2.7.1.95
ExplorEnz Enzyme Link: ExplorEnz 2.7.1.95
PRIAM enzyme-specific profiles Link: PRIAM 2.7.1.95
IntEnz Enzyme Link: IntEnz 2.7.1.95
MEDLINE Enzyme Link: MEDLINE 2.7.1.95

EC number:2.7.1.95

MSA:

2.7.1.95;
Phylogenetic Tree:

2.7.1.95;
Uniprot:
M-CSA:
RHEA:24256 ATP + kanamycin A = ADP + H(+) + kanamycin 3'-phosphate
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8]>>[*:1]-[O;H0;+0:2]-[P;H0;+0:4](=[*:3])(-[*:5])-[*:6].[*:8]-[OH;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Catalytic mechanism of enterococcal kanamycin kinase (APH(3')-IIIa): viscosity, thio, and solvent isotope effects support a Theorell-Chance mechanism.McKay GA, Wright GD1996 Jul 28679630
The crystal structure of aminoglycoside-3'-phosphotransferase-IIa, an enzyme responsible for antibiotic resistance.Nurizzo D, Shewry SC, Perlin MH, Brown SA, Dholakia JN, Fuchs RL, Deva T, Baker EN, Smith CA2003 Mar 2112628253