Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli as a His-tagged fusion protein | Synechocystis sp. |
Protein Variants | Comment | Organism |
---|---|---|
C216A | activity comparable to wild-type, shows a similar redox profile to the wild-type. Analyses of the redox situation of the cysteine using the AMS labeling method reveal two different redox states of the enzyme molecule: wild type and three mutants, C216A, C314A and C340A, show three bands on the gel, oxidized, intermediate and reduced forms, as a function of the redox treatment | Synechocystis sp. |
C314A | activity comparable to wild-type. Analyses of the redox situation of the cysteine using the AMS labeling method reveal two different redox states of the enzyme molecule: wild type and three mutants, C216A, C314A and C340A, show three bands on the gel, oxidized, intermediate and reduced forms, as a function of the redox treatment | Synechocystis sp. |
C314A/C340A | redox change in activity of the double mutant is largely suppressed | Synechocystis sp. |
C340A | activity comparable to wild-type, activity of the mutant C340A is almost insensitive to redox change. Analyses of the redox situation of the cysteine using the AMS labeling method reveal two different redox states of the enzyme molecule: wild type and three mutants, C216A, C314A and C340A, show three bands on the gel, oxidized, intermediate and reduced forms, as a function of the redox treatment | Synechocystis sp. |
C94A | activity comparable to wild-type. Analyses of the redox situation of the cysteine using the AMS labeling method reveal two different redox states of the enzyme molecule. In contrast to wild-type and the mutants, C216A, C314A and C340A, mutants C94A and C97A show only two bands: oxidized and reduced forms, indicating that these mutant form only one disulfide bond | Synechocystis sp. |
C97A | activity comparable to wild-type. Analyses of the redox situation of the cysteine using the AMS labeling method reveal two different redox states of the enzyme molecule. In contrast to wild-type and the mutants, C216A, C314A and C340A, mutants C94A and C97A show only two bands: oxidized and reduced forms, indicating that these mutant form only one disulfide bond | Synechocystis sp. |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.18 | - |
3-phospho-D-glycerate | wild-type, 30°C, pH not specified in the publication | Synechocystis sp. | |
0.19 | - |
ATP | wild-type, 30°C, pH not specified in the publication | Synechocystis sp. |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Synechocystis sp. | the oxidized PGK contains chloroplast-type thioredoxin (Trx)-accessible disulfide bond | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Synechocystis sp. | - |
- |
- |
Purification (Comment) | Organism |
---|---|
using Ni-NTA chromatography | Synechocystis sp. |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 3-phospho-D-glycerate | - |
Synechocystis sp. | ADP + 3-phospho-D-glyceroyl phosphate | - |
r | |
additional information | the oxidized PGK contains chloroplast-type thioredoxin (Trx)-accessible disulfide bond | Synechocystis sp. | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
phosphoglycerate kinase | - |
Synechocystis sp. |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Synechocystis sp. |
General Information | Comment | Organism |
---|---|---|
physiological function | Synechocystis phosphoglycerate kinase is inactivated by oxidation and the oxidized enzyme is easily reduced and reactivated by thioredoxin, suggesting a role for thioredoxin in the control of the redox state of this enzyme | Synechocystis sp. |