The Enzyme Database

Your query returned 3 entries.    printer_iconPrintable version



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
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
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 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
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.  Kudo, F., Hosomi, Y., Tamegai, H. and Kakinuma, K. Purification and characterization of 2-deoxy-scyllo-inosose synthase derived from Bacillus circulans. A crucial carbocyclization enzyme in the biosynthesis of 2-deoxystreptamine-containing aminoglycoside antibiotics. J. Antibiot. (Tokyo) 52 (1999) 81–88. [PMID: 10344560]
3.  Kudo, F., Tamegai, H., Fujiwara, T., Tagami, U., Hirayama, K. and Kakinuma, K. Molecular cloning of the gene for the key carbocycle-forming enzyme in the biosynthesis of 2-deoxystreptamine-containing aminocyclitol antibiotics and its comparison with dehydroquinate synthase. J. Antibiot. (Tokyo) 52 (1999) 559–571. [PMID: 10470681]
4.  Huang, Z., Kakinuma, K. and Eguchi, T. Stereospecificity of hydride transfer in NAD+-catalyzed 2-deoxy-scyllo-inosose synthase, the key enzyme in the biosynthesis of 2-deoxystreptamine-containing aminocyclitol antibiotics. Bioorg. Chem. 33 (2005) 82–89. [DOI] [PMID: 15788164]
5.  Thuy, M.L., Kharel, M.K., Lamichhane, R., Lee, H.C., Suh, J.W., Liou, K. and Sohng, J.K. Expression of 2-deoxy-scyllo-inosose synthase (kanA) from kanamycin gene cluster in Streptomyces lividans. Biotechnol. Lett. 27 (2005) 465–470. [DOI] [PMID: 15928851]
6.  Tamegai, H., Nango, E., Koike-Takeshita, A., Kudo, F. and Kakinuma, K. Significance of the 20-kDa subunit of heterodimeric 2-deoxy-scyllo-inosose synthase for the biosynthesis of butirosin antibiotics in Bacillus circulans. Biosci. Biotechnol. Biochem. 66 (2002) 1538–1545. [PMID: 12224638]
7.  Tamegai, H., Sawada, H., Nango, E., Aoki, R., Hirakawa, H., Iino, T. and Eguchi, T. Roles of a 20 kDa protein associated with a carbocycle-forming enzyme involved in aminoglycoside biosynthesis in primary and secondary metabolism. Biosci. Biotechnol. Biochem. 74 (2010) 1215–1219. [DOI] [PMID: 20530911]
[EC 4.2.3.124 created 2012]
 
 


Data © 2001–2020 IUBMB
Web site © 2005–2020 Andrew McDonald