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Literature summary for 1.2.1.9 extracted from

  • Lebreton, S.; Andreescu, S.; Graciet, E.; Gontero, B.
    Mapping of the interaction site of CP12 with glyceraldehyde-3-phosphate dehydrogenase from Chlamydomonas reinhardtii. Functional consequences for glyceraldehyde-3-phosphate dehydrogenase (2006), FEBS J., 273, 3358-3369.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
chloroplast protein CP12 the chloroplast protein CP12 behaves as a negative regulator of GAPDH activity Chlamydomonas reinhardtii

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
Chlamydomonas reinhardtii 9507
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3-phospho-D-glyceroyl phosphate + NADPH + H+ Chlamydomonas reinhardtii
-
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
?

Organism

Organism UniProt Comment Textmining
Chlamydomonas reinhardtii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant and native GAPDH are purified to apparent homogeneity from Escherichia coli cells and Chlamydomonas reinhardtii, respectively Chlamydomonas reinhardtii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
Chlamydomonas reinhardtii D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
?

Synonyms

Synonyms Comment Organism
GAPDH
-
Chlamydomonas reinhardtii
GAPDH (A4)
-
Chlamydomonas reinhardtii
glyceraldehyde-3-phosphate dehydrogenase
-
Chlamydomonas reinhardtii

Temperature Optimum [┬░C]

Temperature Optimum [┬░C] Temperature Optimum Maximum [┬░C] Comment Organism
30
-
activity assay Chlamydomonas reinhardtii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information catalytic rate constant 238 s-1, control Chlamydomonas reinhardtii
additional information
-
additional information catalytic rate constant 289 s-1, 3 microM 3-phospho-D-glyceroyl phosphate, NADPH-dependent activity of GAPDH in the GAPDH/CP12 complex Chlamydomonas reinhardtii
additional information
-
additional information catalytic rate constant 316 s-1, 160 microM 3-phospho-D-glyceroyl phosphate, NADPH-dependent activity of GAPDH in the GAPDH/CP12 complex Chlamydomonas reinhardtii
additional information
-
additional information catalytic rate constant 330 s-1, 10 microM thioredoxin, NADPH-dependent activity of GAPDH in the GAPDH/CP12 complex Chlamydomonas reinhardtii
additional information
-
additional information catalytic rate constant 390 s-1, 10 microM thioredoxin, 3 microM 3-phospho-D-glyceroyl phosphate, NADPH-dependent activity of GAPDH in the GAPDH/CP12 complex Chlamydomonas reinhardtii
additional information
-
additional information catalytic rate constant 462 s-1, 10 microM thioredoxin, 160 microM 3-phospho-D-glyceroyl phosphate, NADPH-dependent activity of GAPDH in the GAPDH/CP12 complex Chlamydomonas reinhardtii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.9
-
activity assay Chlamydomonas reinhardtii

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Chlamydomonas reinhardtii