EC
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1.14.13.186
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Transferred entry: | 20-oxo-5-O-mycaminosyltylactone 23-monooxygenase. Now EC 1.14.15.34, 20-oxo-5-O-mycaminosyltylactone 23-monooxygenase
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[EC 1.14.13.186 created 2014, deleted 2018] |
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EC |
1.14.15.34 |
Accepted name: |
20-oxo-5-O-mycaminosyltylactone 23-monooxygenase |
Reaction: |
20-oxo-5-O-β-mycaminosyltylactone + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 5-O-β-mycaminosyltylonolide + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O |
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For diagram of tylosin biosynthesis, click here |
Glossary: |
tylactone = (4R,5S,6S,7S,9R,11E,13E,15S,16R)-7,16-diethyl-4,6-dihydroxy-5,9,13,15-tetramethyl-1-oxacyclohexadeca-11,13-diene-2,10-dione
α-D-mycaminose = 3-dimethylamino-3,6-dideoxy-α-D-glucopyranose
tylonolide = 2-[(4R,5S,6S,7R,9R,11E,13E,15R,16R)-16-ethyl-4,6-dihydroxy-15-(hydroxymethyl)-5,9,13-trimethyl-2,10-dioxo-1-oxacyclohexadeca-11,13-dien-7-yl]acetaldehyde |
Other name(s): |
tylH1 (gene name) |
Systematic name: |
20-oxo-5-O-β-mycaminosyltylactone,reduced ferredoxin:oxygen oxidoreductase (23-hydroxylating) |
Comments: |
A cytochrome P-450 (heme-thiolate) protein. Involved in the biosynthetic pathway of the macrolide antibiotic tylosin, which is produced by several species of Streptomyces bacteria. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Baltz, R.H. and Seno, E.T. Properties of Streptomyces fradiae mutants blocked in biosynthesis of the macrolide antibiotic tylosin. Antimicrob. Agents Chemother. 20 (1981) 214–225. [PMID: 7283418] |
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Reeves, C.D., Ward, S.L., Revill, W.P., Suzuki, H., Marcus, M., Petrakovsky, O.V., Marquez, S., Fu, H., Dong, S.D. and Katz, L. Production of hybrid 16-membered macrolides by expressing combinations of polyketide synthase genes in engineered Streptomyces fradiae hosts. Chem. Biol. 11 (2004) 1465–1472. [DOI] [PMID: 15489173] |
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[EC 1.14.15.34 created 2014 as EC 1.14.13.186, transferred 2018 to EC 1.14.15.34] |
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EC |
2.1.1.234 |
Accepted name: |
dTDP-3-amino-3,4,6-trideoxy-α-D-glucopyranose N,N-dimethyltransferase |
Reaction: |
2 S-adenosyl-L-methionine + dTDP-3-amino-3,4,6-trideoxy-α-D-glucopyranose = 2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,4,6-trideoxy-α-D-glucopyranose |
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For diagram of dTDP-D-desosamine biosynthesis, click here |
Glossary: |
α-D-desosamine = 3-dimethylamino-3,4,6-trideoxy-α-D-glucopyranose
dTDP-3-dimethylamino-3,4,6-trideoxy-α-D-glucopyranose = dTDP-D-desosamine |
Other name(s): |
DesVI |
Systematic name: |
S-adenosyl-L-methionine:dTDP-3-amino-3,4,6-trideoxy-α-D-glucopyranose 3-N,N-dimethyltransferase |
Comments: |
The enzyme is involved in the biosynthesis of desosamine, a 3-(dimethylamino)-3,4,6-trideoxyhexose found in certain macrolide antibiotics such as erthyromycin, azithromycin, and clarithromycin. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Chen, H., Yamase, H., Murakami, K., Chang, C.W., Zhao, L., Zhao, Z. and Liu, H.W. Expression, purification, and characterization of two N,N-dimethyltransferases, tylM1 and desVI, involved in the biosynthesis of mycaminose and desosamine. Biochemistry 41 (2002) 9165–9183. [DOI] [PMID: 12119032] |
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Burgie, E.S. and Holden, H.M. Three-dimensional structure of DesVI from Streptomyces venezuelae: a sugar N,N-dimethyltransferase required for dTDP-desosamine biosynthesis. Biochemistry 47 (2008) 3982–3988. [DOI] [PMID: 18327916] |
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[EC 2.1.1.234 created 2011] |
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EC |
2.1.1.235 |
Accepted name: |
dTDP-3-amino-3,6-dideoxy-α-D-glucopyranose N,N-dimethyltransferase |
Reaction: |
2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-α-D-glucopyranose = 2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-α-D-glucopyranose |
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For diagram of dTDP-D-mycaminose biosynthesis, click here |
Glossary: |
dTDP-D-mycaminose = dTDP-3-dimethylamino-3,6-dideoxy-α-D-glucopyranose |
Other name(s): |
TylM1 |
Systematic name: |
S-adenosyl-L-methionine:dTDP-3-amino-3,6-dideoxy-α-D-glucopyranose 3-N,N-dimethyltransferase |
Comments: |
The enzyme is involved in the biosynthesis of mycaminose, an essential structural component of the macrolide antibiotic tylosin, which is produced by the bacterium Streptomyces fradiae. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Chen, H., Yamase, H., Murakami, K., Chang, C.W., Zhao, L., Zhao, Z. and Liu, H.W. Expression, purification, and characterization of two N,N-dimethyltransferases, tylM1 and desVI, involved in the biosynthesis of mycaminose and desosamine. Biochemistry 41 (2002) 9165–9183. [DOI] [PMID: 12119032] |
2. |
Carney, A.E. and Holden, H.M. Molecular architecture of TylM1 from Streptomyces fradiae: an N,N-dimethyltransferase involved in the production of dTDP-D-mycaminose. Biochemistry 50 (2011) 780–787. [DOI] [PMID: 21142177] |
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[EC 2.1.1.235 created 2011] |
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EC |
2.4.1.316 |
Accepted name: |
tylactone mycaminosyltransferase |
Reaction: |
tylactone + dTDP-α-D-mycaminose = dTDP + 5-O-β-D-mycaminosyltylactone |
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For diagram of tylactone biosynthesis, click here |
Glossary: |
tylactone = (4R,5S,6S,7S,9R,11E,13E,15S,16R)-7,16-diethyl-4,6-dihydroxy-5,9,13,15-tetramethyloxacyclohexadeca-11,13-diene-2,10-dione
dTDP-α-D-mycaminose = dTDP-3,6-dideoxy-3-dimethylamino-α-D-glucopyranose |
Other name(s): |
tylM2 (gene name) |
Systematic name: |
dTDP-α-D-mycaminose:tylactone 5-O-β-D-mycaminosyltransferase |
Comments: |
The enzyme participates in the biosynthetic pathway of the macrolide antibiotic tylosin, which is produced by several species of Streptomyces bacteria. Activity is significantly enhanced by the presence of an accessory protein encoded by the tylM3 gene. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Gandecha, A.R., Large, S.L. and Cundliffe, E. Analysis of four tylosin biosynthetic genes from the tylLM region of the Streptomyces fradiae genome. Gene 184 (1997) 197–203. [DOI] [PMID: 9031628] |
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Melancon, C.E., 3rd, Takahashi, H. and Liu, H.W. Characterization of tylM3/tylM2 and mydC/mycB pairs required for efficient glycosyltransfer in macrolide antibiotic biosynthesis. J. Am. Chem. Soc. 126 (2004) 16726–16727. [DOI] [PMID: 15612702] |
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[EC 2.4.1.316 created 2014] |
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EC |
2.4.1.317 |
Accepted name: |
O-mycaminosyltylonolide 6-deoxyallosyltransferase |
Reaction: |
5-O-β-D-mycaminosyltylonolide + dTDP-6-deoxy-α-D-allose = dTDP + demethyllactenocin |
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For diagram of tylosin biosynthesis, click here |
Glossary: |
mycaminose = 3,6-dideoxy-3-dimethylamino-glucopyranose
tylonolide = 2-[(4R,5S,6S,7R,9R,11E,13E,15R,16R)-16-ethyl-4,6-dihydroxy-15-(hydroxymethyl)-5,9,13-trimethyl-2,10-dioxooxacyclohexadeca-11,13-dien-7-yl]acetaldehyde
demethyllactenocin = [(2R,3R,4E,6E,9R,11R,12S,13S,14R)-12-{[3,6-dideoxy-3-(dimethylamino)-D-glucopyranosyl]oxy}-2-ethyl-14-hydroxy-5,9,13-trimethyl-8,16-dioxo-11-(2-oxoethyl)oxacyclohexadeca-4,6-dien-3-yl]methyl 6-deoxy-β-D-allopyranoside |
Other name(s): |
tylN (gene name) |
Systematic name: |
dTDP-6-deoxy-α-D-allose:5-O-β-D-mycaminosyltylonolide 23-O-6-deoxy-α-D-allosyltransferase |
Comments: |
The enzyme participates in the biosynthetic pathway of the macrolide antibiotic tylosin, which is produced by several species of Streptomyces bacteria. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Wilson, V.T. and Cundliffe, E. Characterization and targeted disruption of a glycosyltransferase gene in the tylosin producer, Streptomyces fradiae. Gene 214 (1998) 95–100. [DOI] [PMID: 9651492] |
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[EC 2.4.1.317 created 2014] |
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EC |
2.6.1.89 |
Accepted name: |
dTDP-3-amino-3,6-dideoxy-α-D-glucopyranose transaminase |
Reaction: |
dTDP-3-amino-3,6-dideoxy-α-D-glucopyranose + 2-oxoglutarate = dTDP-3-dehydro-6-deoxy-α-D-glucopyranose + L-glutamate |
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For diagram of dTDP-D-mycaminose biosynthesis, click here |
Glossary: |
dTDP-D-mycaminose = dTDP-3-dimethylamino-3,6-dideoxy-α-D-glucopyranose |
Other name(s): |
TylB; TDP-3-keto-6-deoxy-D-glucose 3-aminotransferase; TDP-3-dehydro-6-deoxy-D-glucose 3-aminotransferase; dTDP-3-keto-6-deoxy-D-glucose 3-aminotransferase; dTDP-3-dehydro-6-deoxy-D-glucose 3-aminotransferase |
Systematic name: |
dTDP-3-amino-3,6-dideoxy-α-D-glucopyranose:2-oxoglutarate aminotransferase |
Comments: |
A pyridoxal-phosphate protein. The reaction occurs in the reverse direction. The enzyme is involved in biosynthesis of D-mycaminose. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Melancon, C.E., 3rd, Hong, L., White, J.A., Liu, Y.N. and Liu, H.W. Characterization of TDP-4-keto-6-deoxy-D-glucose-3,4-ketoisomerase from the D-mycaminose biosynthetic pathway of Streptomyces fradiae: in vitro activity and substrate specificity studies. Biochemistry 46 (2007) 577–590. [DOI] [PMID: 17209568] |
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[EC 2.6.1.89 created 2011] |
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EC |
5.3.2.4 |
Accepted name: |
TDP-4-oxo-6-deoxy-α-D-glucose-3,4-oxoisomerase (dTDP-3-dehydro-6-deoxy-α-D-glucopyranose-forming) |
Reaction: |
dTDP-4-dehydro-6-deoxy-α-D-glucopyranose = dTDP-3-dehydro-6-deoxy-α-D-glucopyranose |
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For diagram of dTDP-D-mycaminose biosynthesis, click here |
Other name(s): |
TDP-4-keto-6-deoxy-D-glucose-3,4-ketoisomerase (ambiguous); Tyl1a; dTDP-4-keto-6-deoxy-D-glucose-3,4-ketoisomerase (ambiguous) |
Systematic name: |
dTDP-4-dehydro-6-deoxy-α-D-glucopyranose:dTDP-3-dehydro-6-deoxy-α-D-glucopyranose isomerase |
Comments: |
The enzyme is involved in biosynthesis of D-mycaminose. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Melancon, C.E., 3rd, Hong, L., White, J.A., Liu, Y.N. and Liu, H.W. Characterization of TDP-4-keto-6-deoxy-D-glucose-3,4-ketoisomerase from the D-mycaminose biosynthetic pathway of Streptomyces fradiae: in vitro activity and substrate specificity studies. Biochemistry 46 (2007) 577–590. [DOI] [PMID: 17209568] |
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[EC 5.3.2.4 created 2011] |
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