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Literature summary for 1.1.1.25 extracted from

  • Rodrigues, V.S.; Breda, A.; Santos, D.S.; Basso, L.A.
    The conserved Lysine69 residue plays a catalytic role in Mycobacterium tuberculosis shikimate dehydrogenase (2009), BMC Res. Notes, 2, 227.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.1.25

Application

Application Comment Organism
drug development the enzyme can be a target for rational design of specific inhibitors, aiming at the development of antitubercular drugs Mycobacterium tuberculosis

Protein Variants

Protein Variants Comment Organism
K69A site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme, overview Mycobacterium tuberculosis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady-state kinetics of wild-type and mutant enzymes, overview Mycobacterium tuberculosis
0.011
-
 NADPH wild-type enzyme, pH 7.3, 25°C Mycobacterium tuberculosis
0.029
-
 3-dehydroshikimate wild-type enzyme, pH 7.3, 25°C Mycobacterium tuberculosis
0.03
-
 NADPH mutant K69A, pH 7.3, 25°C Mycobacterium tuberculosis
0.076
-
 3-dehydroshikimate mutant K69A, pH 7.3, 25°C Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3-dehydroshikimate + NADPH + H+ Mycobacterium tuberculosis
-
 shikimate + NADP+
-
 r

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P95001 gene aroE
-
no activity in Homo sapiens
-
-
-

Reaction

Reaction Comment Organism Reaction ID
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+ catalytic mechanism, residue Lys69 plays a catalytic role and is not involved in substrate binding, overview Mycobacterium tuberculosis
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-dehydroshikimate + NADPH + H+
-
 Mycobacterium tuberculosis shikimate + NADP+
-
 r
3-dehydroshikimate + NADPH + H+ catalytic mechanism, residue Lys69 plays a catalytic role and is not involved in substrate binding Mycobacterium tuberculosis shikimate + NADP+
-
 r

Subunits

Subunits Comment Organism
More three-dimensional structure analysis of wild-type and mutant enzymes with bound substrates, overview Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
MtbSD
-
 Mycobacterium tuberculosis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Mycobacterium tuberculosis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.73
-
 3-dehydroshikimate mutant K69A, pH 7.3, 25°C Mycobacterium tuberculosis
50
-
 3-dehydroshikimate wild-type enzyme, pH 7.3, 25°C Mycobacterium tuberculosis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3
-
 assay at Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
NADP+
-
 Mycobacterium tuberculosis
NADPH
-
 Mycobacterium tuberculosis

General Information

General Information Comment Organism
metabolism aroE-encoded shikimate dehydrogenase catalyzes the forth reaction in the shikimate pathway Mycobacterium tuberculosis
additional information the shikimate pathway is an attractive target for the development of antitubercular agents because it is essential in Mycobacterium tuberculosis, the causative agent of tuberculosis, but absent in humans Mycobacterium tuberculosis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
9.6
-
 3-dehydroshikimate mutant K69A, pH 7.3, 25°C Mycobacterium tuberculosis
24
-
 NADPH mutant K69A, pH 7.3, 25°C Mycobacterium tuberculosis
1700
-
 3-dehydroshikimate wild-type enzyme, pH 7.3, 25°C Mycobacterium tuberculosis
4500
-
 NADPH wild-type enzyme, pH 7.3, 25°C Mycobacterium tuberculosis