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dTDP-4-amino-4,6-dideoxy-alpha-D-glucopyranose + S-adenosyl-L-methionine
dTDP-3-dehydro-4,6-dideoxy-alpha-D-glucopyranose + NH3 + L-methionine + 5'-deoxyadenosine
dTDP-4-amino-4,6-dideoxy-alpha-D-glucopyranose + S-adenosyl-L-methionine + reduced acceptor
dTDP-3-dehydro-4,6-dideoxy-alpha-D-glucopyranose + NH3 + L-methionine + 5'-deoxyadenosine + acceptor
dTDP-4-amino-4,6-dideoxy-D-glucopyranose + S-adenosyl-L-methionine
dTDP-3-dehydro-4,6-dideoxy-alpha-D-glucopyranose + NH3 + L-methionine + 5'-deoxyadenosine
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TDP-4-amino-4-deoxy-D-fucose + S-adenosyl-L-methionine + reduced acceptor
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TDP-4-amino-4-deoxy-D-fucose undergoes deamination alone with a specific activity that is 3fold reduced with respect to deamination of dTDP-4-amino-4,6-dideoxy-alpha-D-glucopyranose. A mechanism is proposed involving direct elimination of ammonium concerted with proton transfer to the nucleofuge from the adjacent alpha-hydroxyalkyl radical
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TDP-D-quinovose + S-adenosyl-L-methionine
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additional information
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dTDP-4-amino-4,6-dideoxy-alpha-D-glucopyranose + S-adenosyl-L-methionine
dTDP-3-dehydro-4,6-dideoxy-alpha-D-glucopyranose + NH3 + L-methionine + 5'-deoxyadenosine
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dTDP-4-amino-4,6-dideoxy-alpha-D-glucopyranose + S-adenosyl-L-methionine
dTDP-3-dehydro-4,6-dideoxy-alpha-D-glucopyranose + NH3 + L-methionine + 5'-deoxyadenosine
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the enzyme is involved in biosynthesis of TDP-D-desosamine
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dTDP-4-amino-4,6-dideoxy-alpha-D-glucopyranose + S-adenosyl-L-methionine
dTDP-3-dehydro-4,6-dideoxy-alpha-D-glucopyranose + NH3 + L-methionine + 5'-deoxyadenosine
the enzyme is involved in biosynthesis of TDP-D-desosamine
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dTDP-4-amino-4,6-dideoxy-alpha-D-glucopyranose + S-adenosyl-L-methionine
dTDP-3-dehydro-4,6-dideoxy-alpha-D-glucopyranose + NH3 + L-methionine + 5'-deoxyadenosine
studies of deuterium incorporation into S-adenosyl-L-methionine using TDP-[3-2H]-4-amino-4,6-dideoxy-D-glucose as the substrate provides strong evidence for direct hydrogen atom transfer to a 5'-deoxyadenosyl radical in the catalytic cycle. The fact that hydrogen atom abstraction occurs at C3 also sheds light on the mechanism of this intriguing deamination reaction. Generation of a 5'-deoxyadenosyl radical is expected to be the first part of the reaction facilitated by the reduced [4Fe-4S]1+ cluster
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dTDP-4-amino-4,6-dideoxy-alpha-D-glucopyranose + S-adenosyl-L-methionine + reduced acceptor
dTDP-3-dehydro-4,6-dideoxy-alpha-D-glucopyranose + NH3 + L-methionine + 5'-deoxyadenosine + acceptor
key reaction in the biosynthesis of TDP-desosamine, which is an essential component of many macrolide antibiotics
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dTDP-4-amino-4,6-dideoxy-alpha-D-glucopyranose + S-adenosyl-L-methionine + reduced acceptor
dTDP-3-dehydro-4,6-dideoxy-alpha-D-glucopyranose + NH3 + L-methionine + 5'-deoxyadenosine + acceptor
the enzyme is involved in the biosynthesis of TDP-desosamine
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dTDP-4-amino-4,6-dideoxy-alpha-D-glucopyranose + S-adenosyl-L-methionine + reduced acceptor
dTDP-3-dehydro-4,6-dideoxy-alpha-D-glucopyranose + NH3 + L-methionine + 5'-deoxyadenosine + acceptor
a mechanism is proposed involving direct elimination of ammonium concerted with proton transfer to the nucleofuge from the adjacent alpha-hydroxyalkyl radical
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dTDP-4-amino-4,6-dideoxy-alpha-D-glucopyranose + S-adenosyl-L-methionine + reduced acceptor
dTDP-3-dehydro-4,6-dideoxy-alpha-D-glucopyranose + NH3 + L-methionine + 5'-deoxyadenosine + acceptor
the radical S-adenosylmethionine enzyme catalyzes the C4-deamination of TDP-4-amino-4,6-dideoxyglucose through a C3 radical intermediate. If the C4 amino group is replaced with a hydroxy group (to give TDP-quinovose), the hydroxy group at C3 is oxidized to a ketone with no C4-dehydration
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additional information
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anaerobic incubation of dTDP-3-keto-6-deoxy-D-glucose (i.e. dTDP-D-quinovose) or dTDP-3-amino-3,6-dideoxy-D-glucose with S-adenosyl-L-methionine and the reconstituted and reduced DesII leads to the formation of dTDP-3-dehydro-6-deoxy-D-glucose. No turnover of dTDP-D-fucose, which contains an axial hydroxyl group at C4, is observed
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additional information
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anaerobic incubation of dTDP-3-keto-6-deoxy-D-glucose (i.e. dTDP-D-quinovose) or dTDP-3-amino-3,6-dideoxy-D-glucose with S-adenosyl-L-methionine and the reconstituted and reduced DesII leads to the formation of dTDP-3-dehydro-6-deoxy-D-glucose. No turnover of dTDP-D-fucose, which contains an axial hydroxyl group at C4, is observed
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additional information
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when the enzyme is incubated with TDP-D-quinovose instead of the natural substrate dTDP-4-amino-4,6-dideoxy-D-glucopyranose, analogous elimination of the C4 hydroxyl is not observed - rather, the C3 hydroxyl is oxidized to the corresponding ketone. EPR characterization of a radical intermediate generated during its catalyzed dehydrogenation of TDP-D-Quinovose
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dTDP-4-amino-4,6-dideoxy-alpha-D-glucopyranose + S-adenosyl-L-methionine
dTDP-3-dehydro-4,6-dideoxy-alpha-D-glucopyranose + NH3 + L-methionine + 5'-deoxyadenosine
dTDP-4-amino-4,6-dideoxy-alpha-D-glucopyranose + S-adenosyl-L-methionine + reduced acceptor
dTDP-3-dehydro-4,6-dideoxy-alpha-D-glucopyranose + NH3 + L-methionine + 5'-deoxyadenosine + acceptor
dTDP-4-amino-4,6-dideoxy-alpha-D-glucopyranose + S-adenosyl-L-methionine
dTDP-3-dehydro-4,6-dideoxy-alpha-D-glucopyranose + NH3 + L-methionine + 5'-deoxyadenosine
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the enzyme is involved in biosynthesis of TDP-D-desosamine
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dTDP-4-amino-4,6-dideoxy-alpha-D-glucopyranose + S-adenosyl-L-methionine
dTDP-3-dehydro-4,6-dideoxy-alpha-D-glucopyranose + NH3 + L-methionine + 5'-deoxyadenosine
the enzyme is involved in biosynthesis of TDP-D-desosamine
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dTDP-4-amino-4,6-dideoxy-alpha-D-glucopyranose + S-adenosyl-L-methionine + reduced acceptor
dTDP-3-dehydro-4,6-dideoxy-alpha-D-glucopyranose + NH3 + L-methionine + 5'-deoxyadenosine + acceptor
key reaction in the biosynthesis of TDP-desosamine, which is an essential component of many macrolide antibiotics
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dTDP-4-amino-4,6-dideoxy-alpha-D-glucopyranose + S-adenosyl-L-methionine + reduced acceptor
dTDP-3-dehydro-4,6-dideoxy-alpha-D-glucopyranose + NH3 + L-methionine + 5'-deoxyadenosine + acceptor
the enzyme is involved in the biosynthesis of TDP-desosamine
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4Fe-4S-center
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a radical S-adenosyl-L-methionine-dependent enzyme. Dependence on a [4Fe-4S] cluster and S-adenosyl-L-methionine for DesII activity
4Fe-4S-center
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[4Fe-4S]1+ is the catalytically active form of all radical S-adenosyl-L-methionine-dependent enzymes. Dependence on a [4Fe-4S] cluster and S-adenosyl-L-methionine for DesII activity
4Fe-4S-center
[4Fe-4S]1+ is the catalytically active form of all radical S-adenosyl-L-methionine-dependent enzymes. Dependence on a [4Fe-4S] cluster and S-adenosyl-L-methionine for DesII activity
S-adenosyl-L-methionine
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a radical S-adenosyl-L-methionine-dependent enzyme. Dependence on a [4Fe-4S] cluster and S-adenosyl-L-methionine for DesII activity
S-adenosyl-L-methionine
a radical S-adenosyl-L-methionine-dependent enzyme. Dependence on a [4Fe-4S] cluster and S-adenosyl-L-methionine for DesII activity
S-adenosyl-L-methionine
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a radical S-adenosyl-L-methionine-dependent enzyme. Dependence on a [4Fe-4S] cluster and S-adenosyl-L-methionine for DesII activity. Radical S-adenosyl-L-methionine enzymes are an important class of biological catalysts involved in radical mediated transformations in both primary and secondary metabolic pathways. All of these enzymes contain a [4Fe-4S] cluster in the active-site and are S-adenosyl-L-methionine dependent. The reactions are initiated by a single electron transfer from the reduced [4Fe-4S]1+ cluster to SAM to induce the homolytic cleavage of the C5'-S bond in -adenosyl-L-methionine, which yields a reactive 5'-deoxyadenosyl radical along with L-methionine. The 5'-deoxyadenosyl radical is used to generate a substrate radical intermediate that is subsequently converted to product
additional information
in the experiment, the [4Fe-4S]2+ of DesII is reduced to [4Fe-4S]1+ by stepwise electron transfer from NADPH through flavodoxin and flavodoxin reductase. Accordingly, a system consisting of flavodoxin/flavodoxin reductase-NADPH or its equivalent from the cellular pool may serve as the in vivo reducing system for the DesII-catalyzed reaction
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additional information
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in the experiment, the [4Fe-4S]2+ of DesII is reduced to [4Fe-4S]1+ by stepwise electron transfer from NADPH through flavodoxin and flavodoxin reductase. Accordingly, a system consisting of flavodoxin/flavodoxin reductase-NADPH or its equivalent from the cellular pool may serve as the in vivo reducing system for the DesII-catalyzed reaction
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0.017
dTDP-4-amino-4,6-dideoxy-alpha-D-glucopyranose
pH 8, 25°C, in presence of 0.1 mM S-adenosyl-L-methionine
additional information
TDP-4-amino-4-deoxy-D-fucose
additional information
TDP-4-amino-4-deoxy-D-fucose
the observed kcat for DesII-catalyzed deamination at pH 8.0 was 3.4fold lower compared to that measured for deamination of the natural substrate dTDP-4-amino-4,6-dideoxy-alpha-D-glucopyranose with the same enzyme preparation
additional information
TDP-4-amino-4-deoxy-D-fucose
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the observed kcat for DesII-catalyzed deamination at pH 8.0 was 3.4fold lower compared to that measured for deamination of the natural substrate dTDP-4-amino-4,6-dideoxy-alpha-D-glucopyranose with the same enzyme preparation
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Szu, P.H.; Ruszczycky, M.W.; Choi, S.H.; Yan, F.; 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
14030-14042
2009
Streptomyces venezuelae (Q9ZGH1), Streptomyces venezuelae
brenda
Ruszczycky, M.W.; Choi, S.H.; 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
2359-2369
2010
Streptomyces venezuelae
brenda
Ruszczycky, M.W.; Choi, S.H.; Mansoorabadi, S.O.; 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
7292-7295
2011
Streptomyces venezuelae
brenda
Ruszczycky, M.W.; Choi, S.H.; Liu, H.W.
EPR-kinetic isotope effect study of the mechanism of radical-mediated dehydrogenation of an alcohol by the radical SAM enzyme DesII
Proc. Natl. Acad. Sci. USA
110
2088-2093
2013
Streptomyces venezuelae (Q9ZGH1), Streptomyces venezuelae
brenda
Ko, Y.; Ruszczycky, M.W.; Choi, S.H.; Liu, H.W.
Mechanistic studies of the radical S-adenosylmethionine enzyme DesII with TDP-D-fucose
Angew. Chem. Int. Ed. Engl.
54
860-863
2015
Streptomyces venezuelae (Q9ZGH1)
brenda
Ko, Y.; Lin, G.M.; Ruszczycky, M.W.; Liu, H.W.
Mechanistic Implications of the Deamination of TDP-4-amino-4-deoxy-d-fucose Catalyzed by the Radical SAM Enzyme DesII
Biochemistry
57
3130-3133
2018
Streptomyces venezuelae (Q9ZGH1), Streptomyces venezuelae
brenda
4.3.1.30 dTDP-4-amino-4,6-dideoxy-D-glucose ammonia-lyase
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