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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

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]
2.	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]

[EC 2.1.1.234 created 2011]

2.6.1.106

Accepted name:

dTDP-3-amino-3,4,6-trideoxy-α-D-glucose transaminase

Reaction:

dTDP-3-amino-3,4,6-trideoxy-α-D-glucose + 2-oxoglutarate = dTDP-3-dehydro-4,6-deoxy-α-D-glucose + L-glutamate

For diagram of dTDP-D-desosamine biosynthesis, click here

Glossary:

dTDP-α-D-desosamine = dTDP-3-(dimethylamino)-3,4,6-trideoxy-α-D-glucose

Other name(s):

desV (gene name); megDII (gene name); eryCI (gene name)

Systematic name:

dTDP-3-amino-3,4,6-trideoxy-α-D-glucose:2-oxoglutarate aminotransferase

Comments:

A pyridoxal-phosphate protein. The enzyme is involved in the biosynthesis of dTDP-α-D-desosamine, a sugar found in several bacterial macrolide antibiotics including erythromycin, megalomicin A, mycinamicin II, and oleandomycin. The reaction occurs in the reverse direction.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Burgie, E.S., Thoden, J.B. and Holden, H.M. Molecular architecture of DesV from Streptomyces venezuelae: a PLP-dependent transaminase involved in the biosynthesis of the unusual sugar desosamine. Protein Sci. 16 (2007) 887–896. [DOI] [PMID: 17456741]

[EC 2.6.1.106 created 2014]

4.3.1.30

Accepted name:

dTDP-4-amino-4,6-dideoxy-D-glucose ammonia-lyase

Reaction:

dTDP-4-amino-4,6-dideoxy-α-D-glucopyranose + S-adenosyl-L-methionine + reduced acceptor = dTDP-3-dehydro-4,6-dideoxy-α-D-glucopyranose + NH₃ + L-methionine + 5′-deoxyadenosine + acceptor

For diagram of dTDP-D-desosamine biosynthesis, click here

Other name(s):

desII (gene name); eryCV (gene name); MegCV

Systematic name:

dTDP-4-amino-4,6-dideoxy-α-D-glucopyranose ammonia lyase (dTDP-3-dehydro-4,6-dideoxy-α-D-glucopyranose-forming)

Comments:

The enzyme, which is a member of the ’AdoMet radical’ (radical SAM) family, is involved in biosynthesis of TDP-α-D-desosamine. The reaction starts by the transfer of an electron from the reduced form of the enzyme’s [4Fe-4S] cluster to S-adenosyl-L-methionine, spliting it into methionine and the radical 5-deoxyadenosin-5′-yl, which attacks the sugar substrate.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Szu, P.H., Ruszczycky, M.W., Choi, S.H., Yan, F. and Liu, H.W. Characterization and mechanistic studies of DesII: a radical S-adenosyl-L-methionine enzyme involved in the biosynthesis of TDP-D-desosamine. J. Am. Chem. Soc. 131 (2009) 14030–14042. [DOI] [PMID: 19746907]
2.	Ruszczycky, M.W., Choi, S.H. and Liu, H.W. Stoichiometry of the redox neutral deamination and oxidative dehydrogenation reactions catalyzed by the radical SAM enzyme DesII. J. Am. Chem. Soc. 132 (2010) 2359–2369. [DOI] [PMID: 20121093]
3.	Ruszczycky, M.W., Choi, S.H., Mansoorabadi, S.O. and Liu, H.W. Mechanistic studies of the radical S-adenosyl-L-methionine enzyme DesII: EPR characterization of a radical intermediate generated during its catalyzed dehydrogenation of TDP-D-quinovose. J. Am. Chem. Soc. 133 (2011) 7292–7295. [DOI] [PMID: 21513273]

[EC 4.3.1.30 created 2011]