The Enzyme Database

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EC 2.1.3.13      
Deleted entry: ATP carbamoyltransferase. The enzyme has been replaced by EC 6.1.2.2, nebramycin 5′ synthase.
[EC 2.1.3.13 created 2013, deleted 2014]
 
 
EC 2.1.3.14      
Deleted entry: tobramycin carbamoyltransferase. The enzyme has been replaced by EC 6.1.2.2, nebramycin 5′ synthase
[EC 2.1.3.14 created 2013, deleted 2014]
 
 
EC 2.3.1.59     
Accepted name: gentamicin 2′-N-acetyltransferase
Reaction: acetyl-CoA + gentamicin C1a = CoA + N2′-acetylgentamicin C1a
Glossary: kanamycin
Other name(s): gentamycin acetyltransferase II; gentamycin 2′-N-acetyltransferase; acetyl-CoA:gentamycin-C1a N2′-acetyltransferase
Systematic name: acetyl-CoA:gentamicin-C1a N2′-acetyltransferase
Comments: The antibiotics gentamicin A, sisomicin, tobramycin, paromomycin, neomycin B, kanamycin B and kanamycin C can also act as acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 50864-40-9
References:
1.  Benveniste, R. and Davies, J. Aminoglycoside antibiotic-inactivating enzymes in actinomycetes similar to those present in clinical isolates of antibiotic-resistant bacteria. Proc. Natl. Acad. Sci. USA 70 (1973) 2276–2280. [DOI] [PMID: 4209515]
[EC 2.3.1.59 created 1976]
 
 
EC 2.3.1.81     
Accepted name: aminoglycoside 3-N-acetyltransferase
Reaction: acetyl-CoA + a 2-deoxystreptamine antibiotic = CoA + N3-acetyl-2-deoxystreptamine antibiotic
For diagram of neamine and ribostamycin biosynthesis, click here
Glossary: kanamycin
Other name(s): 3-aminoglycoside acetyltransferase; 3-N-aminoglycoside acetyltransferase; aminoglycoside N3-acetyltransferase; acetyl-CoA:2-deoxystreptamine-antibiotic N3′-acetyltransferase (incorrect); aminoglycoside N3′-acetyltransferase (incorrect)
Systematic name: acetyl-CoA:2-deoxystreptamine-antibiotic N3-acetyltransferase
Comments: Different from EC 2.3.1.60 gentamicin 3-N-acetyltransferase. A wide range of antibiotics containing the 2-deoxystreptamine ring can act as acceptors, including gentamicin, kanamycin, tobramycin, neomycin and apramycin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 60120-42-5
References:
1.  Davies, J. and O'Connor, S. Enzymatic modification of aminoglycoside antibiotics: 3-N-Acetyltransferase with broad specificity that determines resistance to the novel aminoglycoside apramycin. Antimicrob. Agents Chemother. 14 (1978) 69–72. [PMID: 356726]
[EC 2.3.1.81 created 1984, modified 2015]
 
 
EC 2.3.1.82     
Accepted name: aminoglycoside 6′-N-acetyltransferase
Reaction: acetyl-CoA + kanamycin-B = CoA + N6′-acetylkanamycin-B
Glossary: kanamycin
Other name(s): aminoglycoside N6′-acetyltransferase; aminoglycoside-6′-acetyltransferase; aminoglycoside-6-N-acetyltransferase; kanamycin acetyltransferase
Systematic name: acetyl-CoA:kanamycin-B N6′-acetyltransferase
Comments: The antibiotics kanamycin A, kanamycin B, neomycin, gentamicin C1a, gentamicin C2 and sisomicin are substrates. The antibiotic tobramycin, but not paromomycin, can also act as acceptor. The 6-amino group of the purpurosamine ring is acetylated.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 56467-65-3
References:
1.  le Goffic, F. and Martel, A. La résistance aux aminosides provoquée par une isoenzyme la kanamycine acétyltransférase. Biochimie 56 (1974) 893–897. [DOI] [PMID: 4614862]
2.  Benveniste, R. and Davies, J.E. Enzymatic acetylation of aminoglycoside antibiotics by Escherichia coli carrying an R factor. Biochemistry 10 (1971) 1787–1796. [PMID: 4935296]
3.  Dowding, J.E. Mechanisms of gentamicin resistance in Staphylococcus aureus. Antimicrob. Agents Chemother. 11 (1977) 47–50. [PMID: 836013]
[EC 2.3.1.82 created 1976 as EC 2.3.1.55, transferred 1999 to EC 2.3.1.82, modified 1999, modified 2015]
 
 
EC 2.7.1.190     
Accepted name: aminoglycoside 2′′-phosphotransferase
Reaction: GTP + gentamicin = GDP + gentamicin 2′′-phosphate
Other name(s): aphD (gene name); APH(2′′); aminoglycoside (2′′) kinase; gentamicin kinase (ambiguous); gentamicin phosphotransferase (ambiguous)
Systematic name: GTP:gentamicin 2′′-O-phosphotransferase
Comments: Requires Mg2+. This bacterial enzyme phosphorylates many 4,6-disubstituted aminoglycoside antibiotics that have a hydroxyl group at position 2′′, including kanamycin A, kanamycin B, tobramycin, dibekacin, arbekacin, amikacin, gentamicin C, sisomicin and netilmicin. In most, but not all, cases the phosphorylation confers resistance against the antibiotic. Some forms of the enzyme use ATP as a phosphate donor in appreciable amount. The enzyme is often found as a bifunctional enzyme that also catalyses 6′-aminoglycoside N-acetyltransferase activity. The bifunctional enzyme is the most clinically important aminoglycoside-modifying enzyme in Gram-positive bacteria, responsible for high-level resistance in both Enterococci and Staphylococci.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ferretti, J.J., Gilmore, K.S. and Courvalin, P. Nucleotide sequence analysis of the gene specifying the bifunctional 6′-aminoglycoside acetyltransferase 2"-aminoglycoside phosphotransferase enzyme in Streptococcus faecalis and identification and cloning of gene regions specifying the two activities. J. Bacteriol. 167 (1986) 631–638. [DOI] [PMID: 3015884]
2.  Frase, H., Toth, M. and Vakulenko, S.B. Revisiting the nucleotide and aminoglycoside substrate specificity of the bifunctional aminoglycoside acetyltransferase(6′)-Ie/aminoglycoside phosphotransferase(2′′)-Ia enzyme. J. Biol. Chem. 287 (2012) 43262–43269. [DOI] [PMID: 23115238]
[EC 2.7.1.190 created 2015]
 
 
EC 2.7.7.46     
Accepted name: gentamicin 2′′-nucleotidyltransferase
Reaction: nucleoside triphosphate + gentamicin = diphosphate + 2′′-nucleotidylgentamicin
Other name(s): gentamicin 2′′-adenylyltransferase; aminoglycoside adenylyltransferase; gentamycin 2′′-nucleotidyltransferase
Systematic name: NTP:gentamicin 2′′-nucleotidyltransferase
Comments: ATP, dATP, CTP, ITP and GTP can act as donors; kanamycin, tobramycin and sisomicin can also act as acceptors. The nucleotidyl residue is transferred to the 2-hydroxy of the 3-amino-3-deoxy-D-glucose moiety in the antibiotic.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 62213-33-6
References:
1.  Angelatou, F., Litsas, S.B. and Kontomichalou, P. Purification and properties of two gentamicin-modifying enzymes, coded by a single plasmid pPK237 originating from Pseudomonas aeruginosa. J. Antibiot. 35 (1982) 235–244. [PMID: 6281224]
2.  Naganawa, H., Yagisawa, M., Kondo, S., Takeuchi, T. and Umezawa, H. The structure determination of an enzymatic inactivation product of 3′,4′-dideoxykanamycin B. J. Antibiot. 24 (1971) 913–914. [PMID: 4946513]
3.  Yagisawa, M., Naganawa, H., Kondo, S., Hamada, M., Takeuchi, T. and Umezawa, H. Adenylyldideoxykanamycin B, a product of the inactivation of dideoxykanamycin B by Escherichia coli carrying R factor. J. Antibiot. 24 (1971) 911–912. [PMID: 4946512]
[EC 2.7.7.46 created 1976]
 
 
EC 6.1.2.2     
Accepted name: nebramycin 5′ synthase
Reaction: (1) tobramycin + carbamoyl phosphate + ATP + H2O = nebramycin 5′ + AMP + diphosphate + phosphate (overall reaction)
(1a) carbamoyl phosphate + ATP + H2O = diphosphate + O-carbamoyladenylate + phosphate
(1b) O-carbamoyladenylate + tobramycin = AMP + nebramycin 5′
(2) kanamycin A + carbamoyl phosphate + ATP + H2O = 6′′-O-carbamoylkanamycin A + AMP + diphosphate + phosphate (overall reaction)
(2a) carbamoyl phosphate + ATP + H2O = diphosphate + O-carbamoyladenylate + phosphate
(2b) O-carbamoyladenylate + kanamycin A = AMP + 6′′-O-carbamoylkanamycin A
For diagram of kanamycin A biosynthesis, click here
Glossary: tobramycin = (1S,2S,3R,4S,6R)-4,6-diamino-3-(2,6-diamino-2,3,6-trideoxy-α-D-ribo-hexopyranosyloxy)-2-hydroxycyclohexyl 3-amino-3-deoxy-α-D-glucopyranoside
nebramycin 5′ = (1S,2S,3R,4S,6R)-4,6-diamino-3-[(2,6-diamino-2,3,6-trideoxy-α-D-ribo-hexopyranosyl)oxy]-2-hydroxycyclohexyl 3-amino-6-O-carbamoyl-3-deoxy-α-D-glucopyranoside
kanamycin A = (1S,2R,3R,4S,6R)-4,6-diamino-3-(6-amino-6-deoxy--D-glucopyranosyloxy)-2-hydroxycyclohexyl 3-amino-3-deoxy--D-glucopyranoside
6′′-O-carbamoylkanamycin A = (1S,2R,3R,4S,6R)-4,6-diamino-3-[(6-amino-6-deoxy-α-D-glucopyranosyl)oxy]-2-hydroxycyclohexyl 3-amino-6-O-carbamoyl-3-deoxy-α-D-glucopyranoside
Other name(s): tobramycin carbamoyltransferase; TobZ
Systematic name: tobramycin:carbamoyl phosphate ligase (AMP,phosphate-forming)
Comments: Requires Fe(III). The enzyme from the bacterium Streptoalloteichus tenebrarius catalyses the activation of carbamoyl phosphate to O-carbamoyladenylate and the subsequent carbamoylation of kanamycin and tobramycin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Parthier, C., Gorlich, S., Jaenecke, F., Breithaupt, C., Brauer, U., Fandrich, U., Clausnitzer, D., Wehmeier, U.F., Bottcher, C., Scheel, D. and Stubbs, M.T. The O-carbamoyltransferase TobZ catalyzes an ancient enzymatic reaction. Angew. Chem. Int. Ed. Engl. 51 (2012) 4046–4052. [DOI] [PMID: 22383337]
[EC 6.1.2.2 created 2014]
 
 


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