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Literature summary for 1.1.1.B28 extracted from

  • Wang, Q.; Ding, P.; Perepelov, A.V.; Xu, Y.; Wang, Y.; Knirel, Y.A.; Wang, L.; Feng, L.
    Characterization of the dTDP-D-fucofuranose biosynthetic pathway in Escherichia coli O52 (2008), Mol. Microbiol., 70, 1358-1367.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli BL21 Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Co2+ 5 mM, 11% inhibition Escherichia coli
Cu2+ 5 mM, 88% inhibition Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.38
-
dTDP-4-dehydro-6-deoxy-alpha-D-glucose 37°C, pH 7.4 Escherichia coli
0.84
-
NADH 37°C, pH 7.4 Escherichia coli
0.89
-
NADPH 37°C, pH 7.4 Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
additional information Fcf1 is a divalent cation-independent enzyme Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40700
-
x * 40700, His6-tagged fusion protein, SDS-PAGE Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dTDP-alpha-D-fucopyranose + NADP+ Escherichia coli the enzyme is involved in the dTDP-D-fucofuranose biosynthetic pathway dTDP-4-dehydro-6-deoxy-alpha-D-glucose + NADPH + H+
-
?
dTDP-alpha-D-fucopyranose + NADP+ Escherichia coli O52 the enzyme is involved in the dTDP-D-fucofuranose biosynthetic pathway dTDP-4-dehydro-6-deoxy-alpha-D-glucose + NADPH + H+
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli O52
-
-
-

Purification (Commentary)

Purification (Comment) Organism
His6-tagged fusion protein Escherichia coli

Storage Stability

Storage Stability Organism
-20°C, in 50% glycerol, stable for at least 5 months Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dTDP-alpha-D-fucopyranose + NADH + H+ NADH is a better cofactor than NADPH. kcat/Km for NADH is 4.2fold higher compared to the value for NADPH Escherichia coli dTDP-4-dehydro-6-deoxy-alpha-D-glucose + NAD+
-
?
dTDP-alpha-D-fucopyranose + NADH + H+ NADH is a better cofactor than NADPH. kcat/Km for NADH is 4.2fold higher compared to the value for NADPH Escherichia coli O52 dTDP-4-dehydro-6-deoxy-alpha-D-glucose + NAD+
-
?
dTDP-alpha-D-fucopyranose + NADP+ the enzyme is involved in the dTDP-D-fucofuranose biosynthetic pathway Escherichia coli dTDP-4-dehydro-6-deoxy-alpha-D-glucose + NADPH + H+
-
?
dTDP-alpha-D-fucopyranose + NADP+ the enzyme is involved in the dTDP-D-fucofuranose biosynthetic pathway Escherichia coli O52 dTDP-4-dehydro-6-deoxy-alpha-D-glucose + NADPH + H+
-
?
dTDP-alpha-D-fucopyranose + NADPH + H+ NADH is a better cofactor than NADPH. kcat/Km for NADH is 4.2fold higher compared to the value for NADPH Escherichia coli dTDP-4-dehydro-6-deoxy-alpha-D-glucose + NADP+
-
?
dTDP-alpha-D-fucopyranose + NADPH + H+ NADH is a better cofactor than NADPH. kcat/Km for NADH is 4.2fold higher compared to the value for NADPH Escherichia coli O52 dTDP-4-dehydro-6-deoxy-alpha-D-glucose + NADP+
-
?

Subunits

Subunits Comment Organism
? x * 40700, His6-tagged fusion protein, SDS-PAGE Escherichia coli

Synonyms

Synonyms Comment Organism
dTDP-6-deoxy-D-xylo-hex-4-ulopyranose reductase
-
Escherichia coli
Fcf1
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
15 37
-
Escherichia coli

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
4 50 4°C: 47% of maximal activity, 50°C: 36% of maximal activity Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.78
-
dTDP-4-dehydro-6-deoxy-alpha-D-glucose 37°C, pH 7.4 Escherichia coli
6.76
-
NADPH 37°C, pH 7.4 Escherichia coli
26.67
-
NADH 37°C, pH 7.4 Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NADH NADH is a better cofactor than NADPH. kcat/Km for NADH is 4.2fold higher compared to the value for NADPH Escherichia coli
NADPH NADH is a better cofactor than NADPH. kcat/Km for NADH is 4.2fold higher compared to the value for NADPH Escherichia coli

General Information

General Information Comment Organism
malfunction mutant strains H1862 lacking fcf1. The mutant strain produces semirough lipopolysaccharide with only one O unit attached to the core-lipid A moiety while the wild type strain produces normal lipopolysaccharide. The result indicates that fcf1 is required for the synthesis of the O-antigen in Escherichia coli O52 Escherichia coli
physiological function the enzyme is involved in the biosynthesis of dTDP-D-fucofuranose, a component of the Escherichia coli O52 O-antigen Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
7.4
-
dTDP-4-dehydro-6-deoxy-alpha-D-glucose 37°C, pH 7.4 Escherichia coli
7.6
-
NADPH 37°C, pH 7.4 Escherichia coli
31.75
-
NADH 37°C, pH 7.4 Escherichia coli