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Literature summary for 1.1.1.282 extracted from

  • Michel, G.; Roszak, A.W.; Sauvé, V.; Maclean, J.; Matte, A.; Coggins, J.R.; Cygler, M.; Lapthorn, A.J.
    Structures of shikimate dehydrogenase AroE and its paralog YdiB. A common structural framework for different activitie (2003), J. Biol. Chem., 278, 19463-19472.
    View publication on PubMed
Search for more literature for 1.1.1.282

Crystallization (Commentary)

Crystallization (Comment) Organism
YdiB, with bound cofactors NAD+ or NADP+ Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.02
-
 shikimate pH 9, 20°C, cosubstrate NAD+ Escherichia coli
0.041
-
 L-quinate pH 9, 20°C, cosubstrate NAD+ Escherichia coli
0.087
-
 NAD+ pH 9, 20°C, cosubstrate shikimate Escherichia coli
0.1
-
 NADP+ pH 9, 20°C, cosubstrate shikimate Escherichia coli
0.116
-
 NAD+ pH 9, 20°C, cosubstrate L-quinate Escherichia coli
0.12
-
 shikimate pH 9, 20°C, cosubstrate NADP+ Escherichia coli
0.5
-
 NADP+ pH 9, 20°C, cosubstrate L-quinate Escherichia coli
0.555
-
 L-quinate pH 9, 20°C, cosubstrate NADP+ Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
64000
-
 apoprotein, gel filtration Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli YdiB may be involved in shikimate pathway or may be essential for growth of the organism with quinate as a sole carbon source ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli P0A6D5
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H + H+ reaction mechanism Escherichia coli
a
shikimate + NAD(P)+ = 3-dehydroshikimate + NAD(P)H + H+ reaction mechanism Escherichia coli
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 YdiB has a low specific activity Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-quinate + NAD(P)+ YdiB is a dual specific quinate/shikimate dehydrogenase that utilizes either NAD+ or NADP+ as cofactor, YdiB is equally active with shikimate or quinate, but has a tendency to be more efficient with NAD+ than with NADP+, detailed structure of YdiB, mechanism Escherichia coli 3-dehydroquinate + NAD(P)H + H+
-
 ?
L-quinate + NAD+
-
 Escherichia coli 3-dehydroquinate + NADH + H+
-
 r
additional information YdiB may be involved in shikimate pathway or may be essential for growth of the organism with quinate as a sole carbon source Escherichia coli ?
-
 ?
shikimate + NAD(P)+ YdiB is a dual specific quinate/shikimate dehydrogenase that utilizes either NAD+ or NADP+ as cofactor, YdiB is equally active with shikimate or quinate, but has a tendency to be more efficient with NAD+ than with NADP+, detailed structure of YdiB, mechanism Escherichia coli 3-dehydroshikimate + NAD(P)H + H+ model for 3-dehydroshikimate recognition ?

Subunits

Subunits Comment Organism
dimer
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
20
-
 assay at Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.05
-
 NADP+ pH 9, 20°C, cosubstrate L-quinate Escherichia coli
0.05
-
 shikimate pH 9, 20°C, cosubstrate NAD+ Escherichia coli
0.05
-
 L-quinate pH 9, 20°C, cosubstrate NAD+ or NADP+ Escherichia coli
0.05
-
 NAD+ pH 9, 20°C, cosubstrate shikimate or L-quinate Escherichia coli
0.117
-
 shikimate pH 9, 20°C, cosubstrate NADP+ Escherichia coli
0.117
-
 NADP+ pH 9, 20°C, cosubstrate shikimate Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NAD+ utilizes either NAD+ or NADP+ as a cofactor, tendency to be more efficient with NAD+ than with NADP+, mode of binding Escherichia coli
NADP+ utilizes either NAD+ or NADP+ as a cofactor, tendency to be more efficient with NAD+ than with NADP+, mode of binding Escherichia coli