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Your query returned 10 entries. Printable version
EC | 1.1.1.355 | ||||||
Accepted name: | 2′-dehydrokanamycin reductase | ||||||
Reaction: | kanamycin A + NADP+ = 2′-dehydrokanamycin A + NADPH + H+ | ||||||
For diagram of kanamycin A biosynthesis, click here | |||||||
Glossary: | kanamycin A = (1S,2R,3R,4S,6R)-4,6-diamino-3-(6-amino-6-deoxy-α-D-glucopyranosyloxy)-2-hydroxycyclohexyl 3-amino-3-deoxy-α-D-glucopyranoside 2′-dehydrokanamycin A = (1S,2R,3R,4S,6R)-4,6-diamino-3-[(6-amino-6-deoxy-α-D-arabino-hexopyranosyl-2-ulose)oxy]-2-hydroxycyclohexyl 3-amino-3-deoxy-α-D-glucopyranoside |
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Other name(s): | kanK (gene name, ambiguous) | ||||||
Systematic name: | kanamycin A:NADP+ oxidoreductase | ||||||
Comments: | Found in the bacterium Streptomyces kanamyceticus where it is involved in the conversion of kanamycin B to kanamycin A. | ||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||
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EC | 1.14.11.37 | ||||||
Accepted name: | kanamycin B dioxygenase | ||||||
Reaction: | kanamycin B + 2-oxoglutarate + O2 = 2′-dehydrokanamycin A + succinate + NH3 + CO2 | ||||||
For diagram of kanamycin A biosynthesis, click here | |||||||
Other name(s): | kanJ (gene name) | ||||||
Systematic name: | kanamycin-B,2-oxoglutarate:oxygen oxidoreductase (deaminating, 2′-hydroxylating) | ||||||
Comments: | Requires Fe2+ and ascorbate. Found in the bacterium Streptomyces kanamyceticus where it is involved in the conversion of the aminoglycoside antibiotic kanamycin B to kanamycin A. | ||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||
References: |
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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 The enzyme has been replaced by EC 6.1.2.2, nebramycin 5′ synthase.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 | 2.1.3.14 | ||||||
Deleted entry: | tobramycin carbamoyltransferase. The enzyme has been replaced by EC 6.1.2.2, nebramycin 5′ synthase | ||||||
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: |
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EC | 2.4.1.301 | ||||||
Accepted name: | 2′-deamino-2′-hydroxyneamine 1-α-D-kanosaminyltransferase | ||||||
Reaction: | (1) UDP-α-D-kanosamine + 2′-deamino-2′-hydroxyneamine = UDP + kanamycin A (2) UDP-α-D-kanosamine + neamine = UDP + kanamycin B (3) UDP-α-D-kanosamine + paromamine = UDP + kanamycin C (4) UDP-α-D-kanosamine + 2′-deamino-2′-hydroxyparomamine = UDP + kanamycin X |
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For diagram of kanamycin A biosynthesis, click here | |||||||
Glossary: | neamine = (1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl 2,6-diamino-2,6-dideoxy-α-D-glucopyranoside paromamine = (1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl 2-amino-2-deoxy-α-D-glucopyranoside UDP-α-D-kanosamine = uridine 5′-[3-(3-amino-3-deoxy-α-D-glucopyranosyl) diphosphate] kanamycin A = (1S,2R,3R,4S,6R)-4,6-diamino-3-(6-amino-6-deoxy-α-D-glucopyranosyloxy)-2-hydroxycyclohexyl 3-amino-3-deoxy-α-D-glucopyranoside kanamycin B = (1R,2S,3S,4R,6S)-4,6-diamino-3-(3-amino-3-deoxy-α-D-glucopyranosyloxy)-2-hydroxycyclohexyl 2,6-diamino-2,6-dideoxy-α-D-glucopyranoside kanamycin C = (1R,2S,3S,4R,6S)-4,6-diamino-3-(3-amino-3-deoxy-α-D-glucopyranosyloxy)-2-hydroxycyclohexyl 2-amino-2-deoxy-α-D-glucopyranoside kanamycin X = (1S,2R,3R,4S,6R)-4,6-diamino-3-(α-D-glucopyranosyloxy)-2-hydroxycyclohexyl 3-amino-3-deoxy-α-D-glucopyranoside |
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Other name(s): | kanE (gene name); kanM2 (gene name) | ||||||
Systematic name: | UDP-α-D-kanosamine:2′-deamino-2′-hydroxyneamine 1-α-D-kanosaminyltransferase | ||||||
Comments: | Involved in the biosynthetic pathway of kanamycins. The enzyme characterized from the bacterium Streptomyces kanamyceticus can also accept UDP-α-D-glucose with lower efficiency [2]. | ||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||
References: |
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EC | 2.6.1.93 | ||||||
Accepted name: | neamine transaminase | ||||||
Reaction: | neamine + 2-oxoglutarate = 6′-dehydroparomamine + L-glutamate | ||||||
For diagram of neamine and ribostamycin biosynthesis, click here | |||||||
Other name(s): | glutamate—6′-dehydroparomamine aminotransferase; btrB (gene name); neoN (gene name); kacL (gene name) | ||||||
Systematic name: | neamine:2-oxoglutarate aminotransferase | ||||||
Comments: | The reaction occurs in vivo in the opposite direction. Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin B, butirosin, neomycin and ribostamycin. Works in combination with EC 1.1.3.43, paromamine 6-oxidase, to replace the 6′-hydroxy group of paromamine with an amino group. The enzyme from the bacterium Streptomyces kanamyceticus can also catalyse EC 2.6.1.94, 2′-deamino-2′-hydroxyneamine transaminase, which leads to production of kanamycin A [3]. The enzyme from the bacterium Streptomyces fradiae can also catalyse EC 2.6.1.95, leading to production of neomycin C [2]. | ||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||
References: |
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EC | 2.6.1.94 | ||||||
Accepted name: | 2′-deamino-2′-hydroxyneamine transaminase | ||||||
Reaction: | 2′-deamino-2′-hydroxyneamine + 2-oxoglutarate = 2′-deamino-2′-hydroxy-6′-dehydroparomamine + L-glutamate | ||||||
Other name(s): | kacL (gene name) | ||||||
Systematic name: | 2′-deamino-2′-hydroxyneamine:2-oxoglutarate aminotransferase | ||||||
Comments: | The reaction occurs in vivo in the opposite direction. Involved in the biosynthetic pathway of kanamycin A and kanamycin D. The enzyme, characterized from the bacterium Streptomyces kanamyceticus, can also catalyse EC 2.6.1.93, neamine transaminase. | ||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||
References: |
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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, PDB | ||||||
References: |
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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 |
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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 |
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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, PDB | ||||||
References: |
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