BRENDA - Enzyme Database
show all sequences of 4.2.1.68

Evolution of enzymatic activities in the enolase superfamily: L-fuconate dehydratase from Xanthomonas campestris

Yew, W.S.; Fedorov, A.A.; Fedorov, E.V.; Rakus, J.F.; Pierce, R.W.; Almo, S.C.; Gerlt, J.A.; Biochemistry 45, 14582-14597 (2006)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
-
Xanthomonas campestris
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.33
-
L-fuconate
25°C, pH 7.5
Xanthomonas campestris
2.1
-
D-Arabinonate
25°C, pH 7.5
Xanthomonas campestris
6.2
-
L-galactonate
25°C, pH 7.5
Xanthomonas campestris
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Xanthomonas campestris
-
pv. campestris str. ATCC 33913
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-altronate
-
678170
Xanthomonas campestris
?
-
-
-
?
D-arabinonate
dehydration of D-arabinonate is initiated by abstraction of the 2-proton by Lys220
678170
Xanthomonas campestris
?
-
-
-
?
D-ribonate
dehydrations of D-ribonate is initiated by abstraction of the 2-proton by His351
678170
Xanthomonas campestris
?
-
-
-
?
L-fuconate
FucD reaction involves initial abstraction of the 2-proton by Lys220, acid catalysis of the vinylogous beta-elimination of the 3-OH group by His351, and stereospecific ketonization of the resulting enol, likely by the conjugate acid of Lys220, to yield the 2-keto-3-deoxy-L-fuconate product
678170
Xanthomonas campestris
2-dehydro-3-deoxy-L-fuconate + H2O
-
-
-
?
L-galactonate
dehydration of L-galactonate is initiated by abstraction of the 2-proton by Lys220
678170
Xanthomonas campestris
2-keto-3-deoxy-L-galactonate + H2O
-
-
-
?
L-talonate
dehydrations of L-talonate is initiated by abstraction of the 2-proton by His351
678170
Xanthomonas campestris
?
-
-
-
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.9
-
L-galactonate
25°C, pH 7.5
Xanthomonas campestris
2.4
-
D-Arabinonate
25°C, pH 7.5
Xanthomonas campestris
15
-
L-fuconate
25°C, pH 7.5
Xanthomonas campestris
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Xanthomonas campestris
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.33
-
L-fuconate
25°C, pH 7.5
Xanthomonas campestris
2.1
-
D-Arabinonate
25°C, pH 7.5
Xanthomonas campestris
6.2
-
L-galactonate
25°C, pH 7.5
Xanthomonas campestris
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-altronate
-
678170
Xanthomonas campestris
?
-
-
-
?
D-arabinonate
dehydration of D-arabinonate is initiated by abstraction of the 2-proton by Lys220
678170
Xanthomonas campestris
?
-
-
-
?
D-ribonate
dehydrations of D-ribonate is initiated by abstraction of the 2-proton by His351
678170
Xanthomonas campestris
?
-
-
-
?
L-fuconate
FucD reaction involves initial abstraction of the 2-proton by Lys220, acid catalysis of the vinylogous beta-elimination of the 3-OH group by His351, and stereospecific ketonization of the resulting enol, likely by the conjugate acid of Lys220, to yield the 2-keto-3-deoxy-L-fuconate product
678170
Xanthomonas campestris
2-dehydro-3-deoxy-L-fuconate + H2O
-
-
-
?
L-galactonate
dehydration of L-galactonate is initiated by abstraction of the 2-proton by Lys220
678170
Xanthomonas campestris
2-keto-3-deoxy-L-galactonate + H2O
-
-
-
?
L-talonate
dehydrations of L-talonate is initiated by abstraction of the 2-proton by His351
678170
Xanthomonas campestris
?
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.9
-
L-galactonate
25°C, pH 7.5
Xanthomonas campestris
2.4
-
D-Arabinonate
25°C, pH 7.5
Xanthomonas campestris
15
-
L-fuconate
25°C, pH 7.5
Xanthomonas campestris
Other publictions for EC 4.2.1.68
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
747890
Motter
Categorisation of sugar acid ...
Aspergillus niger, Aspergillus niger ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7
Fungal Genet. Biol.
64
67-72
2014
-
-
1
-
-
-
-
3
-
-
-
-
-
2
-
-
-
-
-
-
-
-
13
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
13
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
678170
Yew
Evolution of enzymatic activit ...
Xanthomonas campestris
Biochemistry
45
14582-14597
2006
-
-
1
-
-
-
-
3
-
-
-
-
-
5
-
-
-
-
-
-
-
-
6
-
-
-
-
3
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
33953
Veiga
-
L.Fuconate dehydratase: purifi ...
Aureobasidium pullulans
Arq. Biol. Tecnol.
34
537-553
1991
-
-
-
-
-
1
11
2
-
-
2
1
-
1
-
-
1
-
-
-
1
1
3
-
1
1
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
1
-
11
-
2
-
-
2
1
-
-
-
1
-
-
1
1
3
-
1
1
-
-
1
1
-
-
-
-
-
-
-
-
33952
Chan
L-Fucose metabolism in mammals ...
Sus scrofa
J. Biol. Chem.
254
7060-7068
1979
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
3
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
3
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
33951
Yuen
L-Fucose metabolism in mammals ...
Sus scrofa
Can. J. Biochem.
50
798-806
1972
-
-
-
-
-
-
1
2
-
1
-
1
-
1
-
-
1
-
-
1
1
1
3
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
1
-
1
-
-
-
1
-
1
1
1
3
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-