EC |
1.1.1.329 |
Accepted name: |
2-deoxy-scyllo-inosamine dehydrogenase |
Reaction: |
2-deoxy-scyllo-inosamine + NAD(P)+ = 3-amino-2,3-dideoxy-scyllo-inosose + NAD(P)H + H+ |
|
For diagram of paromamine biosynthesis, click here |
Glossary: |
2-deoxy-scyllo-inosamine = (1R,2S,3S,4R,5S)-5-aminocyclohexane-1,2,3,4-tetrol |
Other name(s): |
neoA (gene name); kanK (gene name, ambiguous); kanE (gene name, ambiguous) |
Systematic name: |
2-deoxy-scyllo-inosamine:NAD(P)+ 1-oxidoreductase |
Comments: |
Requires zinc. Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, neomycin and ribostamycin. cf. EC 1.1.99.38, 2-deoxy-scyllo-inosamine dehydrogenase (AdoMet-dependent). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Kudo, F., Yamamoto, Y., Yokoyama, K., Eguchi, T. and Kakinuma, K. Biosynthesis of 2-deoxystreptamine by three crucial enzymes in Streptomyces fradiae NBRC 12773. J. Antibiot. (Tokyo) 58 (2005) 766–774. [DOI] [PMID: 16506694] |
2. |
Nepal, K.K., Oh, T.J. and Sohng, J.K. Heterologous production of paromamine in Streptomyces lividans TK24 using kanamycin biosynthetic genes from Streptomyces kanamyceticus ATCC12853. Mol. Cells 27 (2009) 601–608. [DOI] [PMID: 19466609] |
|
[EC 1.1.1.329 created 2012] |
|
|
|
|
EC |
1.1.3.43 |
Accepted name: |
paromamine 6′-oxidase |
Reaction: |
paromamine + O2 = 6′-dehydroparomamine + H2O2 |
Other name(s): |
btrQ (gene name); neoG (gene name); kanI (gene name); tacB (gene name); neoQ (obsolete gene name) |
Systematic name: |
paromamine:oxygen 6′-oxidoreductase |
Comments: |
Contains FAD. Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin. Works in combination with EC 2.6.1.93, neamine transaminase, to replace the 6′-hydroxy group of paromamine with an amino group. The enzyme from the bacterium Streptomyces fradiae also catalyses EC 1.1.3.44, 6′′′-hydroxyneomycin C oxidase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Huang, F., Spiteller, D., Koorbanally, N.A., Li, Y., Llewellyn, N.M. and Spencer, J.B. Elaboration of neosamine rings in the biosynthesis of neomycin and butirosin. ChemBioChem 8 (2007) 283–288. [DOI] [PMID: 17206729] |
2. |
Yu, Y., Hou, X., Ni, X. and Xia, H. Biosynthesis of 3′-deoxy-carbamoylkanamycin C in a Streptomyces tenebrarius mutant strain by tacB gene disruption. J. Antibiot. (Tokyo) 61 (2008) 63–69. [DOI] [PMID: 18408324] |
3. |
Clausnitzer, D., Piepersberg, W. and Wehmeier, U.F. The oxidoreductases LivQ and NeoQ are responsible for the different 6′-modifications in the aminoglycosides lividomycin and neomycin. J. Appl. Microbiol. 111 (2011) 642–651. [DOI] [PMID: 21689223] |
|
[EC 1.1.3.43 created 2012] |
|
|
|
|
EC |
1.1.3.44 |
Accepted name: |
6′′′-hydroxyneomycin C oxidase |
Reaction: |
6′′′-deamino-6′′′-hydroxyneomycin C + O2 = 6′′′-deamino-6′′′-oxoneomycin C + H2O2 |
Other name(s): |
neoG (gene name); neoQ (obsolete gene name) |
Systematic name: |
6′′′-deamino-6′′′-hydroxyneomycin C:oxygen 6′′′-oxidoreductase |
Comments: |
Contains FAD. Involved in the biosynthetic pathway of aminoglycoside antibiotics of the neomycin family. Works in combination with EC 2.6.1.95, neomycin C transaminase, to replace the 6′′′-hydroxy group of 6′′′-hydroxyneomycin C with an amino group.
Also catalyses EC 1.1.3.43, paromamine 6′-oxidase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Huang, F., Spiteller, D., Koorbanally, N.A., Li, Y., Llewellyn, N.M. and Spencer, J.B. Elaboration of neosamine rings in the biosynthesis of neomycin and butirosin. ChemBioChem 8 (2007) 283–288. [DOI] [PMID: 17206729] |
2. |
Clausnitzer, D., Piepersberg, W. and Wehmeier, U.F. The oxidoreductases LivQ and NeoQ are responsible for the different 6′-modifications in the aminoglycosides lividomycin and neomycin. J. Appl. Microbiol. 111 (2011) 642–651. [DOI] [PMID: 21689223] |
|
[EC 1.1.3.44 created 2012] |
|
|
|
|
EC |
1.1.99.38 |
Accepted name: |
2-deoxy-scyllo-inosamine dehydrogenase (AdoMet-dependent) |
Reaction: |
2-deoxy-scyllo-inosamine + S-adenosyl-L-methionine = 3-amino-2,3-dideoxy-scyllo-inosose + 5′-deoxyadenosine + L-methionine |
|
For diagram of paromamine biosynthesis, click here |
Other name(s): |
btrN (gene name); 2-deoxy-scyllo-inosamine dehydrogenase (SAM-dependent) |
Systematic name: |
2-deoxy-scyllo-inosamine:S-adenosyl-L-methionine 1-oxidoreductase |
Comments: |
Involved in the biosynthetic pathway of the aminoglycoside antibiotics of the butirosin family. The enzyme from Bacillus circulans was shown to be a radical S-adenosyl-L-methionine (SAM) enzyme. cf. EC 1.1.1.329, 2-deoxy-scyllo-inosamine dehydrogenase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Yokoyama, K., Numakura, M., Kudo, F., Ohmori, D. and Eguchi, T. Characterization and mechanistic study of a radical SAM dehydrogenase in the biosynthesis of butirosin. J. Am. Chem. Soc. 129 (2007) 15147–15155. [DOI] [PMID: 18001019] |
2. |
Yokoyama, K., Ohmori, D., Kudo, F. and Eguchi, T. Mechanistic study on the reaction of a radical SAM dehydrogenase BtrN by electron paramagnetic resonance spectroscopy. Biochemistry 47 (2008) 8950–8960. [DOI] [PMID: 18672902] |
|
[EC 1.1.99.38 created 2012, modified 2013] |
|
|
|
|
EC |
2.4.1.283 |
Accepted name: |
2-deoxystreptamine N-acetyl-D-glucosaminyltransferase |
Reaction: |
UDP-N-acetyl-α-D-glucosamine + 2-deoxystreptamine = UDP + 2′-N-acetylparomamine |
|
For diagram of paromamine biosynthesis, click here |
Other name(s): |
btrM (gene name); neoD (gene name); kanF (gene name) |
Systematic name: |
UDP-N-acetyl-α-D-glucosamine:2-deoxystreptamine N-acetyl-D-glucosaminyltransferase |
Comments: |
Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin. Unlike the enzyme from the bacterium Streptomyces kanamyceticus, which can also accept UDP-D-glucose [2] (cf. EC 2.4.1.284, 2-deoxystreptamine glucosyltransferase), the enzyme from Bacillus circulans can only accept UDP-N-acetyl-α-D-glucosamine [1]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Yokoyama, K., Yamamoto, Y., Kudo, F. and Eguchi, T. Involvement of two distinct N-acetylglucosaminyltransferases and a dual-function deacetylase in neomycin biosynthesis. ChemBioChem 9 (2008) 865–869. [DOI] [PMID: 18311744] |
2. |
Park, J.W., Park, S.R., Nepal, K.K., Han, A.R., Ban, Y.H., Yoo, Y.J., Kim, E.J., Kim, E.M., Kim, D., Sohng, J.K. and Yoon, Y.J. Discovery of parallel pathways of kanamycin biosynthesis allows antibiotic manipulation. Nat. Chem. Biol. 7 (2011) 843–852. [DOI] [PMID: 21983602] |
|
[EC 2.4.1.283 created 2012] |
|
|
|
|
EC |
2.4.1.284 |
Accepted name: |
2-deoxystreptamine glucosyltransferase |
Reaction: |
UDP-α-D-glucose + 2-deoxystreptamine = UDP + 2′-deamino-2′-hydroxyparomamine |
Glossary: |
2′-deamino-2′-hydroxyparomamine = 4-O-α-D-glucopyranosyl-2-deoxy-D-streptamine |
Other name(s): |
kanF (gene name) |
Systematic name: |
UDP-α-D-glucose:2-deoxystreptamine 6-α-D-glucosyltransferase |
Comments: |
Involved in the biosynthesis of kanamycin B and kanamycin C. Also catalyses EC 2.4.1.283, 2-deoxystreptamine N-acetyl-D-glucosaminyltransferase, but activity is only one fifth of that with UDP-α-D-glucose. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Park, J.W., Park, S.R., Nepal, K.K., Han, A.R., Ban, Y.H., Yoo, Y.J., Kim, E.J., Kim, E.M., Kim, D., Sohng, J.K. and Yoon, Y.J. Discovery of parallel pathways of kanamycin biosynthesis allows antibiotic manipulation. Nat. Chem. Biol. 7 (2011) 843–852. [DOI] [PMID: 21983602] |
|
[EC 2.4.1.284 created 2012] |
|
|
|
|
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 |
|
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 |
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: |
1. |
Kudo, F., Sucipto, H. and Eguchi, T. Enzymatic activity of a glycosyltransferase KanM2 encoded in the kanamycin biosynthetic gene cluster. J. Antibiot. (Tokyo) 62 (2009) 707–710. [DOI] [PMID: 19911031] |
2. |
Park, J.W., Park, S.R., Nepal, K.K., Han, A.R., Ban, Y.H., Yoo, Y.J., Kim, E.J., Kim, E.M., Kim, D., Sohng, J.K. and Yoon, Y.J. Discovery of parallel pathways of kanamycin biosynthesis allows antibiotic manipulation. Nat. Chem. Biol. 7 (2011) 843–852. [DOI] [PMID: 21983602] |
|
[EC 2.4.1.301 created 2013] |
|
|
|
|
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: |
1. |
Huang, F., Spiteller, D., Koorbanally, N.A., Li, Y., Llewellyn, N.M. and Spencer, J.B. Elaboration of neosamine rings in the biosynthesis of neomycin and butirosin. ChemBioChem 8 (2007) 283–288. [DOI] [PMID: 17206729] |
2. |
Clausnitzer, D., Piepersberg, W. and Wehmeier, U.F. The oxidoreductases LivQ and NeoQ are responsible for the different 6′-modifications in the aminoglycosides lividomycin and neomycin. J. Appl. Microbiol. 111 (2011) 642–651. [DOI] [PMID: 21689223] |
3. |
Park, J.W., Park, S.R., Nepal, K.K., Han, A.R., Ban, Y.H., Yoo, Y.J., Kim, E.J., Kim, E.M., Kim, D., Sohng, J.K. and Yoon, Y.J. Discovery of parallel pathways of kanamycin biosynthesis allows antibiotic manipulation. Nat. Chem. Biol. 7 (2011) 843–852. [DOI] [PMID: 21983602] |
|
[EC 2.6.1.93 created 2012] |
|
|
|
|
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: |
1. |
Park, J.W., Park, S.R., Nepal, K.K., Han, A.R., Ban, Y.H., Yoo, Y.J., Kim, E.J., Kim, E.M., Kim, D., Sohng, J.K. and Yoon, Y.J. Discovery of parallel pathways of kanamycin biosynthesis allows antibiotic manipulation. Nat. Chem. Biol. 7 (2011) 843–852. [DOI] [PMID: 21983602] |
|
[EC 2.6.1.94 created 2012] |
|
|
|
|
EC |
2.6.1.100 |
Accepted name: |
L-glutamine:2-deoxy-scyllo-inosose aminotransferase |
Reaction: |
L-glutamine + 2-deoxy-scyllo-inosose = 2-oxoglutaramate + 2-deoxy-scyllo-inosamine |
|
For diagram of paromamine biosynthesis, click here |
Glossary: |
2-deoxy-scyllo-inosose = (2S,3R,4S,5R)-2,3,4,5-tetrahydroxycyclohexan-1-one |
Other name(s): |
btrR (gene name); neoB (gene name); kanB (gene name) |
Systematic name: |
L-glutamine:2-deoxy-scyllo-inosose aminotransferase |
Comments: |
Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin. Also catalyses EC 2.6.1.101, L-glutamine:5-amino-2,3,4-trihydroxycyclohexanone aminotransferase [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Tamegai, H., Eguchi, T. and Kakinuma, K. First identification of Streptomyces genes involved in the biosynthesis of 2-deoxystreptamine-containing aminoglycoside antibiotics--genetic and evolutionary analysis of L-glutamine:2-deoxy-scyllo-inosose aminotransferase genes. J. Antibiot. (Tokyo) 55 (2002) 1016–1018. [PMID: 12546424] |
2. |
Huang, F., Haydock, S.F., Mironenko, T., Spiteller, D., Li, Y. and Spencer, J.B. The neomycin biosynthetic gene cluster of Streptomyces fradiae NCIMB 8233: characterisation of an aminotransferase involved in the formation of 2-deoxystreptamine. Org. Biomol. Chem. 3 (2005) 1410–1418. [DOI] [PMID: 15827636] |
3. |
Kudo, F., Yamamoto, Y., Yokoyama, K., Eguchi, T. and Kakinuma, K. Biosynthesis of 2-deoxystreptamine by three crucial enzymes in Streptomyces fradiae NBRC 12773. J. Antibiot. (Tokyo) 58 (2005) 766–774. [DOI] [PMID: 16506694] |
4. |
Jnawali, H.N., Subba, B., Liou, K. and Sohng, J.K. Functional characterization of kanB by complementing in engineered Streptomyces fradiae Δneo6::tsr. Biotechnol. Lett. 31 (2009) 869–875. [DOI] [PMID: 19219581] |
|
[EC 2.6.1.100 created 2013] |
|
|
|
|
EC |
2.6.1.101 |
Accepted name: |
L-glutamine:3-amino-2,3-dideoxy-scyllo-inosose aminotransferase |
Reaction: |
L-glutamine + 3-amino-2,3-dideoxy-scyllo-inosose = 2-oxoglutaramate + 2-deoxystreptamine |
|
For diagram of paromamine biosynthesis, click here |
Glossary: |
3-amino-2,3-dideoxy-scyllo-inosose = (2R,3S,4R,5S)-5-amino-2,3,4-trihydroxycyclohexan-1-one |
Systematic name: |
L-glutamine:5-amino-2,3,4-trihydroxycyclohexanone aminotransferase |
Comments: |
Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin. Also catalyses EC 2.6.1.100, L-glutamine:2-deoxy-scyllo-inosose aminotransferase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Huang, F., Haydock, S.F., Mironenko, T., Spiteller, D., Li, Y. and Spencer, J.B. The neomycin biosynthetic gene cluster of Streptomyces fradiae NCIMB 8233: characterisation of an aminotransferase involved in the formation of 2-deoxystreptamine. Org. Biomol. Chem. 3 (2005) 1410–1418. [DOI] [PMID: 15827636] |
2. |
Kudo, F., Yamamoto, Y., Yokoyama, K., Eguchi, T. and Kakinuma, K. Biosynthesis of 2-deoxystreptamine by three crucial enzymes in Streptomyces fradiae NBRC 12773. J. Antibiot. (Tokyo) 58 (2005) 766–774. [DOI] [PMID: 16506694] |
|
[EC 2.6.1.101 created 2013] |
|
|
|
|
EC |
2.7.1.95 |
Accepted name: |
kanamycin kinase |
Reaction: |
ATP + kanamycin = ADP + kanamycin 3′-phosphate |
Glossary: |
kanamycin |
Other name(s): |
neomycin-kanamycin phosphotransferase; |
Systematic name: |
ATP:kanamycin 3′-O-phosphotransferase |
Comments: |
Also acts on the antibiotics neomycin, paromomycin, neamine, paromamine, vistamycin and gentamicin A. An enzyme from Pseudomonas aeruginosa also acts on butirosin. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 62213-36-9 |
References: |
1. |
Doi, O., Ogura, M., Tanaka, N. and Umezawa, H. Inactivation of kanamycin, neomycin, and streptomycin by enzymes obtained in cells of Pseudomonas aeruginosa. Appl. Microbiol. 16 (1968) 1276–1281. [PMID: 4970990] |
2. |
Dolin, M.I. The Streptococcus faecalis oxidases for reduced diphosphopyridine nucleotide. III. Isolation and properties of a flavin peroxidase for reduced diphosphopyridine nucleotide. J. Biol. Chem. 225 (1957) 557–573. [PMID: 13416259] |
|
[EC 2.7.1.95 created 1976] |
|
|
|
|
EC |
3.5.1.112 |
Accepted name: |
2′-N-acetylparomamine deacetylase |
Reaction: |
2′-N-acetylparomamine + H2O = paromamine + acetate |
|
For diagram of paromamine biosynthesis, click here |
Glossary: |
paromamine = (1R)-O4-(2-amino-2-deoxy-α-D-glucopyranosyl)-2-deoxy-streptamine |
Other name(s): |
btrD (gene name); neoL (gene name); kanN (gene name) |
Systematic name: |
2′-N-acetylparomamine hydrolase (acetate-forming) |
Comments: |
Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin. The enzyme from the bacterium Streptomyces fradiae can also accept 2′′′-acetyl-6′′′-hydroxyneomycin C as substrate, cf. EC 3.5.1.113, 2′′′-acetyl-6′′′-hydroxyneomycin C deacetylase [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Truman, A.W., Huang, F., Llewellyn, N.M. and Spencer, J.B. Characterization of the enzyme BtrD from Bacillus circulans and revision of its functional assignment in the biosynthesis of butirosin. Angew. Chem. Int. Ed. Engl. 46 (2007) 1462–1464. [DOI] [PMID: 17226887] |
2. |
Yokoyama, K., Yamamoto, Y., Kudo, F. and Eguchi, T. Involvement of two distinct N-acetylglucosaminyltransferases and a dual-function deacetylase in neomycin biosynthesis. ChemBioChem 9 (2008) 865–869. [DOI] [PMID: 18311744] |
|
[EC 3.5.1.112 created 2012] |
|
|
|
|
EC |
3.5.1.113 |
Accepted name: |
2′′′-acetyl-6′′′-hydroxyneomycin C deacetylase |
Reaction: |
2′′′-acetyl-6′′′-deamino-6′′′-hydroxyneomycin C + H2O = 6′′′-deamino-6′′′-hydroxyneomycin C + acetate |
Other name(s): |
neoL (gene name) |
Systematic name: |
2′′′-acetyl-6′′′-hydroxyneomycin C hydrolase (acetate-forming) |
Comments: |
Involved in the biosynthetic pathway of aminoglycoside antibiotics of the neomycin family. The enzyme from the bacterium Streptomyces fradiae also catalyses EC 3.5.1.112, 2′-N-acetylparomamine deacetylase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Yokoyama, K., Yamamoto, Y., Kudo, F. and Eguchi, T. Involvement of two distinct N-acetylglucosaminyltransferases and a dual-function deacetylase in neomycin biosynthesis. ChemBioChem 9 (2008) 865–869. [DOI] [PMID: 18311744] |
|
[EC 3.5.1.113 created 2012] |
|
|
|
|
EC |
4.2.3.124 |
Accepted name: |
2-deoxy-scyllo-inosose synthase |
Reaction: |
D-glucose 6-phosphate = 2-deoxy-L-scyllo-inosose + phosphate |
|
For diagram of paromamine biosynthesis, click here |
Other name(s): |
btrC (gene name); neoC (gene name); kanC (gene name) |
Systematic name: |
D-glucose-6-phosphate phosphate-lyase (2-deoxy-L-scyllo-inosose-forming) |
Comments: |
Requires Co2+ [2]. Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin. Requires an NAD+ cofactor, which is transiently reduced during the reaction [1,4]. The enzyme from the bacterium Bacillus circulans forms a complex with the glutamine amidotransferase subunit of pyridoxal 5′-phosphate synthase (EC 4.3.3.6), which appears to stabilize the complex [6,7]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Kudo, F., Yamauchi, N., Suzuki, R. and Kakinuma, K. Kinetic isotope effect and reaction mechanism of 2-deoxy-scyllo-inosose synthase derived from butirosin-producing Bacillus circulans. J. Antibiot. (Tokyo) 50 (1997) 424–428. [PMID: 9207913] |
2. |
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