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Literature summary for 2.7.2.3 extracted from

  • Tsukamoto, Y.; Fukushima, Y.; Hara, S.; Hisbori, T.
    Redox control of the activity of phosphoglycerate kinase in Synechocystis sp. PCC6803 (2013), Plant Cell Physiol., 54, 484-491.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli as a His-tagged fusion protein Synechocystis sp.

Protein Variants

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 [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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Synechocystis sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
using Ni-NTA chromatography Synechocystis sp.

Substrates and Products (Substrate)

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

Synonyms Comment Organism
phosphoglycerate kinase
-
Synechocystis sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Synechocystis sp.

General Information

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.