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Literature summary extracted from

  • Mukherjee, S.; Dutta, D.; Saha, B.; Das, A.K.
    Crystal structure of glyceraldehyde-3-phosphate dehydrogenase 1 from methicillin-resistant Staphylococcus aureus MRSA252 provides novel insights into substrate binding and catalytic mechanism (2010), J. Mol. Biol., 401, 949-968.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.2.1.12 wild type holo and apoenzymes and mutant enzymes C151S, C151G and C151S/H178N in complex with NAD+ and D-glyceraldehyde 3-phosphate, hanging drop vapor diffusion method, the wild-type holoenzyme and apoenzyme are crystallized from 0.1 M Tris-HCl, pH 8.5, and 20% (w/v) PEG 4000 at 4°C and from 0.1 M Tris-HCl, pH 8.2, and 32% (w/v) PEG 3350 at 25°C, respectively. Crystals of active-site mutants in complex with NAD+ (C151S, C151G, and C151S/H178N) grow at 25°C from 0.1 M Tris-HCl, pH 8.5, and 28% (w/v) PEG 4000, from 0.1 M Tris-HCl, pH 8.2, and 30% (w/v) PEG 4000, and from 0.1 M Tris-HCl, pH 8.5, and 30% (w/v) PEG 4000, respectively, while mutant H178N in complex with NAD+ crystallizes from 0.1 M Tris-HCl, pH 8.2, and 30% (w/v) PEG 4000 at 4°C Staphylococcus aureus

Protein Variants

EC Number Protein Variants Comment Organism
1.2.1.12 C151/H178N the rate of the forward reaction is decreased by 47000 times compared to the wild type enzyme with similar affinity for the substrate and the coenzyme Staphylococcus aureus
1.2.1.12 C151G the mutant is completely inactive Staphylococcus aureus
1.2.1.12 C151S the mutant shows drastically reduced kcat values compared to the wild type enzyme Staphylococcus aureus
1.2.1.12 H178N the mutant shows no significant difference in the Km values of D-glyceraldehyde 3-phosphate, phosphate, and NAD+ compared to the wild type enzyme, however, the mutation results in the reduction of kcat of oxidative phosphorylation by 1400times Staphylococcus aureus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.12 0.31
-
 D-glyceraldehyde 3-phosphate wild type enzyme, pH 8.7, 25°C Staphylococcus aureus
1.2.1.12 0.32
-
 D-glyceraldehyde 3-phosphate mutant enzyme H178N, pH 8.7, 25°C Staphylococcus aureus
1.2.1.12 0.34
-
 D-glyceraldehyde 3-phosphate mutant enzyme C151S, pH 8.7, 25°C Staphylococcus aureus
1.2.1.12 0.34
-
 D-glyceraldehyde 3-phosphate mutant enzyme C151S/H178N, pH 8.7, 25°C Staphylococcus aureus
1.2.1.12 2.54
-
 phosphate wild type enzyme, pH 8.7, 25°C Staphylococcus aureus
1.2.1.12 3.03
-
 phosphate mutant enzyme H178N, pH 8.7, 25°C Staphylococcus aureus
1.2.1.12 3.09
-
 phosphate mutant enzyme C151S, pH 8.7, 25°C Staphylococcus aureus
1.2.1.12 3.68
-
 phosphate mutant enzyme C151S/H178N, pH 8.7, 25°C Staphylococcus aureus
1.2.1.12 312
-
 NAD+ mutant enzyme C151S/H178N, pH 8.7, 25°C Staphylococcus aureus
1.2.1.12 316
-
 NAD+ wild type enzyme, pH 8.7, 25°C Staphylococcus aureus
1.2.1.12 320
-
 NAD+ mutant enzyme H178N, pH 8.7, 25°C Staphylococcus aureus
1.2.1.12 322
-
 NAD+ mutant enzyme C151S, pH 8.7, 25°C Staphylococcus aureus

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.12 Staphylococcus aureus Q6GIL8
-
-
1.2.1.12 Staphylococcus aureus MRSA252 Q6GIL8
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.12 D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
 Staphylococcus aureus 3-phospho-D-glyceroyl phosphate + NADH
-
 ?
1.2.1.12 D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
 Staphylococcus aureus MRSA252 3-phospho-D-glyceroyl phosphate + NADH
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.1.12 homotetramer x-ray crystallography Staphylococcus aureus

Synonyms

EC Number Synonyms Comment Organism
1.2.1.12 GAPDH1
-
 Staphylococcus aureus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.2.1.12 25
-
-
 Staphylococcus aureus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2.1.12 0.002
-
 D-glyceraldehyde 3-phosphate mutant enzyme C151S/H178N, pH 8.7, 25°C Staphylococcus aureus
1.2.1.12 0.05
-
 D-glyceraldehyde 3-phosphate mutant enzyme H178N, pH 8.7, 25°C Staphylococcus aureus
1.2.1.12 0.09
-
 D-glyceraldehyde 3-phosphate mutant enzyme C151S, pH 8.7, 25°C Staphylococcus aureus
1.2.1.12 70
-
 D-glyceraldehyde 3-phosphate wild type enzyme, pH 8.7, 25°C Staphylococcus aureus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.1.12 8.7
-
-
 Staphylococcus aureus

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.12 NAD+
-
 Staphylococcus aureus