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Literature summary for 1.1.1.282 extracted from

  • Peek, J.; Christendat, D.
    The shikimate dehydrogenase family: functional diversity within a conserved structural and mechanistic framework (2015), Arch. Biochem. Biophys., 566, 85-99.
    View publication on PubMed
Search for more literature for 1.1.1.282

Application

Application Comment Organism
drug development the essential enzyme is a potential target for herbicides and antimicrobials Corynebacterium glutamicum

Cloned(Commentary)

Cloned (Comment) Organism
gene cgR_0495, recombinant expression Corynebacterium glutamicum
gene qsuD, recombinant expression Corynebacterium glutamicum

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure analysis of binary and ternary complexes of enzyme and substrates, PDB IDs 3JYP, 2NLO, 3JYO, and 3JYQ Corynebacterium glutamicum
crystal structure determination as enzyme in binary complex with NAD+ (PDB ID 3JYO), or in ternary complex with shikimate and NADH (PDB ID 3JYQ), or in ternary complex with quinate and NADH (PDB ID 3JYP) Corynebacterium glutamicum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.018
-
 NAD+ with shikimate, pH 8.6, 30°C Corynebacterium glutamicum
0.187
-
 shikimate with NADP+, pH 7.0, 30°C Corynebacterium glutamicum
0.2
-
 3-dehydroshikimate with NADPH, pH 7.0, 30°C Corynebacterium glutamicum
0.26
-
 shikimate with NAD+, pH 8.6, 30°C Corynebacterium glutamicum
2.541
-
 L-quinate with NADPH, pH 7.0, 30°C 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+
-
 r
L-quinate + NAD+ Corynebacterium glutamicum ATCC 13032
-
 3-dehydroquinate + NADH + H+
-
 r
L-quinate + NADP+ Corynebacterium glutamicum
-
 3-dehydroquinate + NADPH + H+
-
 r
shikimate + NAD+ Corynebacterium glutamicum
-
 3-dehydroshikimate + NADH + H+
-
 r
shikimate + NAD+ Corynebacterium glutamicum ATCC 13032
-
 3-dehydroshikimate + NADH + H+
-
 r
shikimate + NADP+ Corynebacterium glutamicum
-
 3-dehydroshikimate + NADPH + H+
-
 r

Organism

Organism UniProt Comment Textmining
Corynebacterium glutamicum A4QB65
-
-
Corynebacterium glutamicum Q9X5C9
-
-
Corynebacterium glutamicum ATCC 13032 Q9X5C9
-
-

Reaction

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-quinate + NAD+
-
 Corynebacterium glutamicum 3-dehydroquinate + NADH + H+
-
 r
L-quinate + NAD+
-
 Corynebacterium glutamicum ATCC 13032 3-dehydroquinate + NADH + H+
-
 r
L-quinate + NADP+
-
 Corynebacterium glutamicum 3-dehydroquinate + NADPH + H+
-
 r
additional information the enzyme is capable of recognizing both quinate and shikimate, it is usually considered to have dual substrate specificity Corynebacterium glutamicum ?
-
 ?
additional information the enzyme is capable of recognizing both quinate and shikimate, it is usually considered to have dual substrate specificity Corynebacterium glutamicum ATCC 13032 ?
-
 ?
shikimate + NAD+
-
 Corynebacterium glutamicum 3-dehydroshikimate + NADH + H+
-
 r
shikimate + NAD+
-
 Corynebacterium glutamicum ATCC 13032 3-dehydroshikimate + NADH + H+
-
 r
shikimate + NADP+
-
 Corynebacterium glutamicum 3-dehydroshikimate + NADPH + H+
-
 r

Subunits

Subunits Comment Organism
dimer
-
 Corynebacterium glutamicum

Synonyms

Synonyms Comment Organism
quinate/shikimate dehydrogenase
-
 Corynebacterium glutamicum

Temperature Optimum [°C]

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.036
-
 L-quinate with NADPH, pH 7.0, 30°C Corynebacterium glutamicum
9.6
-
 shikimate with NAD+, pH 8.6, 30°C Corynebacterium glutamicum
31.1
-
 shikimate with NADP+, pH 7.0, 30°C Corynebacterium glutamicum
329
-
 3-dehydroshikimate with NADPH, pH 7.0, 30°C Corynebacterium glutamicum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Corynebacterium glutamicum
8.6
-
 assay at Corynebacterium glutamicum

Cofactor

Cofactor Comment Organism Structure
NAD+ dependent on Corynebacterium glutamicum
NADH dependent on Corynebacterium glutamicum
NADP+
-
 Corynebacterium glutamicum
NADPH
-
 Corynebacterium glutamicum

General Information

General Information Comment Organism
evolution SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences Corynebacterium glutamicum
malfunction disruption of the qdh gene in prevents growth on both compounds, demonstrating the important role of the enzyme in hydroaromatic catabolism Corynebacterium glutamicum
metabolism the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites Corynebacterium glutamicum
physiological function shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes. The reduced efficiency of Corynebacterium glutamicum enzyme with shikimate as a substrate may also result in part from the flexibility of the catalytic group, Lys73, which adopts multiple conformations in the shikimate-liganded enzyme structure Corynebacterium glutamicum