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Literature summary 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

Application

EC Number Application Comment Organism
1.1.1.25 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

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.25 additional information
-
additional information steady-state kinetics of wild-type and mutant enzymes, overview Mycobacterium tuberculosis
1.1.1.25 0.011
-
NADPH wild-type enzyme, pH 7.3, 25°C Mycobacterium tuberculosis
1.1.1.25 0.029
-
3-dehydroshikimate wild-type enzyme, pH 7.3, 25°C Mycobacterium tuberculosis
1.1.1.25 0.03
-
NADPH mutant K69A, pH 7.3, 25°C Mycobacterium tuberculosis
1.1.1.25 0.076
-
3-dehydroshikimate mutant K69A, pH 7.3, 25°C Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.25 3-dehydroshikimate + NADPH + H+ Mycobacterium tuberculosis
-
shikimate + NADP+
-
r

Organism

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

Reaction

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.25 3-dehydroshikimate + NADPH + H+
-
Mycobacterium tuberculosis shikimate + NADP+
-
r
1.1.1.25 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

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

Synonyms

EC Number Synonyms Comment Organism
1.1.1.25 MtbSD
-
Mycobacterium tuberculosis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.25 25
-
assay at Mycobacterium tuberculosis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.25 0.73
-
3-dehydroshikimate mutant K69A, pH 7.3, 25°C Mycobacterium tuberculosis
1.1.1.25 50
-
3-dehydroshikimate wild-type enzyme, pH 7.3, 25°C Mycobacterium tuberculosis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.25 7.3
-
assay at Mycobacterium tuberculosis

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.25 NADP+
-
Mycobacterium tuberculosis
1.1.1.25 NADPH
-
Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
1.1.1.25 metabolism aroE-encoded shikimate dehydrogenase catalyzes the forth reaction in the shikimate pathway Mycobacterium tuberculosis
1.1.1.25 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]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.1.25 9.6
-
3-dehydroshikimate mutant K69A, pH 7.3, 25°C Mycobacterium tuberculosis
1.1.1.25 24
-
NADPH mutant K69A, pH 7.3, 25°C Mycobacterium tuberculosis
1.1.1.25 1700
-
3-dehydroshikimate wild-type enzyme, pH 7.3, 25°C Mycobacterium tuberculosis
1.1.1.25 4500
-
NADPH wild-type enzyme, pH 7.3, 25°C Mycobacterium tuberculosis