Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Schoepe, J.; Niefind, K.; Schomburg, D.
    1.6 A structure of an NAD(+)-dependent quinate dehydrogenase from Corynebacterium glutamicum (2008), Acta Crystallogr. Sect. D, 64, 803-809.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.24 NAD+-dependent enzyme, X-ray diffraction structure determination and anaylsis at 1.64-8.0 A resolution, molecular replacement method, modelling of the ternary complexes, overview Corynebacterium glutamicum
1.1.1.25 diffraction to 1.6 A Corynebacterium glutamicum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.24 10.2
-
 L-quinate pH 9.0, 30°C Corynebacterium glutamicum
1.1.1.24 46.6
-
 shikimate pH 10.0, 30°C Corynebacterium glutamicum
1.1.1.25 10.2
-
 quinate pH 9.0, 30°C Corynebacterium glutamicum
1.1.1.25 46.6
-
 shikimate pH 10.0, 30°C Corynebacterium glutamicum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.24 L-quinate + NAD+ Corynebacterium glutamicum QDH plays a key role in the quinate-degradation pathway 3-dehydroquinate + NADH + H+
-
 r
1.1.1.24 shikimate + NAD+ Corynebacterium glutamicum
-
 3-dehydroshikimate + NADH + H+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.24 Corynebacterium glutamicum
-
 ORF Cgl0424
-
1.1.1.25 Corynebacterium glutamicum Q9X5C9 quinate/shikimate dehydrogenase
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.25 shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+ active-site base is K92. After the binding of quinate and NAD+, the oxygen of the C3-OH of quinate forms a hydrogen bond to the side chain of the conserved T88 and K92 functions as the active-site base to remove the proton on the C3-OH. Simultaneously,a hydride is transferred from C3 of quinate to NAD+ Corynebacterium glutamicum
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.24 L-quinate + NAD+ QDH plays a key role in the quinate-degradation pathway Corynebacterium glutamicum 3-dehydroquinate + NADH + H+
-
 r
1.1.1.24 L-quinate + NAD+ Thr88 and Thr221 are involved in quinate binding Corynebacterium glutamicum 3-dehydroquinate + NADH + H+
-
 r
1.1.1.24 additional information structure of the potential binding site of quinate and shikimate includign the the completely conserved residues Lys92 and Asp102, overview. The crystal structure reveals that in contrast to shikimate, quinate forms a hydrogen bond to the NAD+. In addition, the hydroxyl group of a conserved active-site threonine hydrogen binds to quinate more effectively than to shikimate. Also, the hydroxyl group of a conserved tyrosine approaches the carboxylate group of quinate more closely than it does the carboxylate group of shikimate, active site structure, overview Corynebacterium glutamicum ?
-
 ?
1.1.1.24 shikimate + NAD+
-
 Corynebacterium glutamicum 3-dehydroshikimate + NADH + H+
-
 r
1.1.1.25 quinate + NAD+ in contrast to shikimate, quinate may form a hydrogen bond to the NAD+, and the hydroxyl group of a active-site threonine hydrogen bonds to quinate more effectively than shikimate resulting in a lower Michaelis constant and higher catalytic efficiency for quinate Corynebacterium glutamicum 3-dehydroquinate + NADH + H+
-
 ?
1.1.1.25 shikimate + NAD+
-
 Corynebacterium glutamicum 3-dehydroshikimate + NADH + H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.24 More seconfdary and tertiary enzyme structures, the enzyme is composed of two alphabetaalpha domains containing two discontinuous segments, Asp22-Asn127 and Gly287-Leu302, overview Corynebacterium glutamicum

Synonyms

EC Number Synonyms Comment Organism
1.1.1.24 More the enzyme belongs to a functional class of the shikimate/quinate dehydrogenase family Corynebacterium glutamicum
1.1.1.24 NAD+-dependent QDH
-
 Corynebacterium glutamicum
1.1.1.24 NAD+-dependent quinate dehydrogenase
-
 Corynebacterium glutamicum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.24 30
-
 assay at Corynebacterium glutamicum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.24 61.9
-
 L-quinate pH 9.0, 30°C Corynebacterium glutamicum
1.1.1.24 85.2
-
 shikimate pH 10.0, 30°C Corynebacterium glutamicum
1.1.1.25 61.9
-
 quinate pH 9.0, 30°C Corynebacterium glutamicum
1.1.1.25 85.2
-
 shikimate pH 10.0, 30°C Corynebacterium glutamicum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.24 9
-
 quinate dehydrogenase activity Corynebacterium glutamicum
1.1.1.24 10
-
 shikimate dehydrogenase activity Corynebacterium glutamicum

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.24 NAD+ dependent on, 300fold higher activity compared to NADP+ Corynebacterium glutamicum
1.1.1.24 NADH binding site structure, overview Corynebacterium glutamicum
1.1.1.25 NAD+ preferred over NADP+ Corynebacterium glutamicum
1.1.1.25 NADP+ turnover number decreases by more than 300fold when NADP+ is used instead of NAD+, regardless of substrate shikimate or quinate Corynebacterium glutamicum