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Literature summary for 4.3.1.30 extracted from

  • 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 (2009), J. Am. Chem. Soc., 131, 14030-14042.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.3.1.30

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.05
-
 dTDP-4-amino-4,6-dideoxy-alpha-D-glucopyranose pH 8, 25°C, in presence of 0.1 mM S-adenosyl-L-methionine Streptomyces venezuelae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
48000
-
 gel filtration Streptomyces venezuelae
54265
-
 1 * 54265, His-tag-DesII, His-tag-DesII is a monomer in solution. It is not clear that the observed monomeric state is due to the presence of the His-tag, calculated from sequence Streptomyces venezuelae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dTDP-4-amino-4,6-dideoxy-alpha-D-glucopyranose + S-adenosyl-L-methionine Streptomyces venezuelae the enzyme is involved in biosynthesis of TDP-D-desosamine dTDP-3-dehydro-4,6-dideoxy-alpha-D-glucopyranose + NH3 + L-methionine + 5'-deoxyadenosine
-
 ?

Organism

Organism UniProt Comment Textmining
Streptomyces venezuelae Q9ZGH1
-
-

Purification (Commentary)

Purification (Comment) Organism
purification of C-terminal His6-tagged DesII from Escherichia coli BL21 Star (DE3)-desII/pET24 cells Streptomyces venezuelae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dTDP-4-amino-4,6-dideoxy-alpha-D-glucopyranose + S-adenosyl-L-methionine the enzyme is involved in biosynthesis of TDP-D-desosamine Streptomyces venezuelae 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 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 Streptomyces venezuelae dTDP-3-dehydro-4,6-dideoxy-alpha-D-glucopyranose + NH3 + L-methionine + 5'-deoxyadenosine
-
 ?
additional information 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 Streptomyces venezuelae ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 54265, His-tag-DesII, His-tag-DesII is a monomer in solution. It is not clear that the observed monomeric state is due to the presence of the His-tag, calculated from sequence Streptomyces venezuelae

Synonyms

Synonyms Comment Organism
DesII
-
 Streptomyces venezuelae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Streptomyces venezuelae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
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 Streptomyces venezuelae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Streptomyces venezuelae

Cofactor

Cofactor Comment Organism Structure
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 Streptomyces venezuelae
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 Streptomyces venezuelae
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 Streptomyces venezuelae

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.33
-
 dTDP-4-amino-4,6-dideoxy-alpha-D-glucopyranose pH 8, 25°C, in presence of 0.1 mM S-adenosyl-L-methionine Streptomyces venezuelae