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

BRENDA support

Literature summary for 1.1.1.25 extracted from

  • Avitia-Dominguez, C.; Sierra-Campos, E.; Salas-Pacheco, J.M.; Najera, H.; Rojo-Dominguez, A.; Cisneros-Martinez, J.; Tellez-Valencia, A.
    Inhibition and biochemical characterization of methicillin-resistant Staphylococcus aureus shikimate dehydrogenase: an in silico and kinetic study (2014), Molecules, 19, 4491-4509.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.1.25

Application

Application Comment Organism
drug development the enzyme is a target for antibacterial drug development Staphylococcus aureus

Cloned(Commentary)

Cloned (Comment) Organism
gene aroE, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS Staphylococcus aureus

Inhibitors

Inhibitors Comment Organism Structure
2,2'-bithiophene-5-carboxylic acid the inhibitor is identified by virtual screeening, 87% inhibition at 0.2 mM, competitive versus shikimate, uncompetitive versus NADP+. Flexible docking studies reveal that the inhibitor molecule makes interactions with catalytic residues Staphylococcus aureus
2-[4-(trifluoromethyl)phenyl]-1,3-thiazole-4-carboxylic acid 31% inhibition at 0.2 mM Staphylococcus aureus
2-[methyl[3-(trifluoromethyl)naphthalen-1-yl]amino]ethan-1-ol 49% inhibition at 0.2 mM Staphylococcus aureus
3-ethyl-3,4-dihydro-2H-1-benzopyran 31% inhibition at 0.2 mM Staphylococcus aureus
4-[(morpholin-4-yl)methyl]benzoic acid 31% inhibition at 0.2 mM Staphylococcus aureus
5-(hex-1-yn-1-yl)furan-2-carboxylic acid 29% inhibition at 0.2 mM Staphylococcus aureus
6-hydroxy-2,3-dihydrobenzo[b]furan-3-one the inhibitor is identified by virtual screeening, 99% inhibition at 0.2 mM, mixed-type inhibition versus shikimate, uncompetitive versus NADP+. Flexible docking studies reveal that the inhibitor molecule makes interactions with catalytic residues Staphylococcus aureus
7-hydroxy-2,2,8-trimethyl-2,3-dihydro-4H-chromen-4-one the inhibitor is identified by virtual screeening, 87% inhibition at 0.2 mM, competitive versus shikimate, uncompetitive versus NADP+. Flexible docking studies reveal that the inhibitor molecule makes interactions with catalytic residues Staphylococcus aureus
methyl 3-hydroxy-1-benzothiophene-2-carboxylate 33% inhibition at 0.2 mM Staphylococcus aureus
[2-[2-(dimethylamino)ethoxy]phenyl]methanol 45% inhibition at 0.2 mM Staphylococcus aureus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information the enzyme shows Michaelis-Menten kinetics toward both substrates shikimate and NADP+, kinetic analysis, sequential random mechanism, overview Staphylococcus aureus
0.03746
-
 shikimate pH not specified in the publication, 25°C Staphylococcus aureus
0.04255
-
 NADP+ pH not specified in the publication, 25°C Staphylococcus aureus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
29000
-
 gel filtration Staphylococcus aureus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
shikimate + NADP+ Staphylococcus aureus
-
 3-dehydroshikimate + NADPH + H+
-
 ?
shikimate + NADP+ Staphylococcus aureus ATCC MRSA252
-
 3-dehydroshikimate + NADPH + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus
-
-
-
Staphylococcus aureus ATCC MRSA252
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography Staphylococcus aureus

Reaction

Reaction Comment Organism Reaction ID
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+ the enzyme catalysis follows a sequential random mechanism, enzyme catalysis depends on acid-basic amino acids Staphylococcus aureus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
shikimate + NADP+
-
 Staphylococcus aureus 3-dehydroshikimate + NADPH + H+
-
 ?
shikimate + NADP+
-
 Staphylococcus aureus ATCC MRSA252 3-dehydroshikimate + NADPH + H+
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 29000, SDS-PAGE Staphylococcus aureus
More three-dimensional structure determination by homology modelling and validation Staphylococcus aureus

Synonyms

Synonyms Comment Organism
AroE
-
 Staphylococcus aureus
SDH
-
 Staphylococcus aureus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65
-
-
 Staphylococcus aureus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
10 60 activity range, maximum activity at 65°C, inactivation at 70°C Staphylococcus aureus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
135.8
-
 shikimate pH not specified in the publication, 25°C Staphylococcus aureus
146.2
-
 NADP+ pH not specified in the publication, 25°C Staphylococcus aureus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9 11
-
 Staphylococcus aureus

pH Range

pH Minimum pH Maximum Comment Organism
6.5 12.5 activity range, overview Staphylococcus aureus

Cofactor

Cofactor Comment Organism Structure
NADP+
-
 Staphylococcus aureus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
 additional information kinetic study of the enzyme-inhibitor complexes Staphylococcus aureus

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3430
-
 NADP+ pH not specified in the publication, 25°C Staphylococcus aureus
3620
-
 shikimate pH not specified in the publication, 25°C Staphylococcus aureus