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Literature summary for 1.1.1.282 extracted from

  • Kubota, T.; Tanaka, Y.; Hiraga, K.; Inui, M.; Yukawa, H.
    Characterization of shikimate dehydrogenase homologues of Corynebacterium glutamicum (2013), Appl. Microbiol. Biotechnol., 97, 8139-8149.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene qsuD, recombinant expression in Escherichia coli Corynebacterium glutamicum

Protein Variants

Protein Variants Comment Organism
additional information construction of a gene qsuD deletion mutant. Cell cultures of the qsuD-deficient strain in glucose-containing medium are light yellow, whereas those of the wild-type in shikimate or quinate-containing medium are brown Corynebacterium glutamicum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis constant with quinate as substrate is lower than that with shikimate under optimal conditions Corynebacterium glutamicum
0.42
-
3-dehydroquinate pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADH Corynebacterium glutamicum
0.444
-
L-quinate pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+ Corynebacterium glutamicum
1.141
-
3-dehydroquinate pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADPH Corynebacterium glutamicum
1.299
-
shikimate pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+ Corynebacterium glutamicum
5.933
-
3-dehydroshikimate pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADH Corynebacterium glutamicum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
30000
-
-
Corynebacterium glutamicum
60000
-
about, gel filtration Corynebacterium glutamicum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-quinate + NAD+ Corynebacterium glutamicum
-
3-dehydroquinate + NADH + H+
-
?
shikimate + NAD+ Corynebacterium glutamicum
-
3-dehydroshikimate + NADH + H+
-
?
shikimate + NAD+ Corynebacterium glutamicum JCM 18229
-
3-dehydroshikimate + NADH + H+
-
?

Organism

Organism UniProt Comment Textmining
Corynebacterium glutamicum A4QB65
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli Corynebacterium glutamicum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-quinate + NAD+
-
Corynebacterium glutamicum 3-dehydroquinate + NADH + H+
-
?
additional information QsuD reduces 3-dehydroquinate using NADH and oxidizes quinate using NAD+ as cofactor Corynebacterium glutamicum ?
-
?
additional information QsuD reduces 3-dehydroquinate using NADH and oxidizes quinate using NAD+ as cofactor Corynebacterium glutamicum JCM 18229 ?
-
?
shikimate + NAD+
-
Corynebacterium glutamicum 3-dehydroshikimate + NADH + H+
-
?
shikimate + NAD+
-
Corynebacterium glutamicum JCM 18229 3-dehydroshikimate + NADH + H+
-
?

Subunits

Subunits Comment Organism
homodimer 2 * 30000, about, recombinant enzyme, SDS-PAGE Corynebacterium glutamicum

Synonyms

Synonyms Comment Organism
cgR_0495
-
Corynebacterium glutamicum
qsuD
-
Corynebacterium glutamicum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.75
-
shikimate pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+ Corynebacterium glutamicum
5.67
-
3-dehydroshikimate pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADH Corynebacterium glutamicum
9.31
-
3-dehydroquinate pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADPH Corynebacterium glutamicum
14.6
-
L-quinate pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+ Corynebacterium glutamicum
114
-
3-dehydroquinate pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADH Corynebacterium glutamicum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
reduction of 3-dehydroquinate with NADH Corynebacterium glutamicum
8.5
-
oxidation of quinate with NAD+ Corynebacterium glutamicum

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
the catalytic reaction of QsuD is highly susceptible to pH Corynebacterium glutamicum

Cofactor

Cofactor Comment Organism Structure
additional information the turnover number is lower with NADP+ instead of NAD+ as cofactor. NADP(H) is just only for 3-dehydroquinate reduction by the enzyme Corynebacterium glutamicum
NAD+
-
Corynebacterium glutamicum
NADH
-
Corynebacterium glutamicum

Expression

Organism Comment Expression
Corynebacterium glutamicum qsuD mRNA expression is upregulated in shikimate-grown cells relative to that in the glucose-grown cells up

General Information

General Information Comment Organism
physiological function QsuD is essential for growth on shikimate and quinate as sole carbon sources, suggesting that it is the key enzyme for shikimate/quinate utilization Corynebacterium glutamicum

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.96
-
3-dehydroshikimate pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADH Corynebacterium glutamicum
1.35
-
shikimate pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+ Corynebacterium glutamicum
8.16
-
3-dehydroquinate pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADPH Corynebacterium glutamicum
32.88
-
L-quinate pH 7.0, temperature not specified in the publication, recombinant enzyme, with NAD+ Corynebacterium glutamicum
271.4
-
3-dehydroquinate pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADH Corynebacterium glutamicum