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Literature summary for 2.7.2.3 extracted from

  • Lin, M.; Turpin, D.H.
    Purification and characterization of two forms of phosphoglycerate kinase from the green algae Selenastrum minutum (1993), J. Phycol., 29, 777-786.
No PubMed abstract available
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics Monoraphidium minutum
0.32
-
 ATP isozyme PGK2, pH 7.3-7.8 Monoraphidium minutum
0.32
-
 ATP ATP in form of MgATP2- Monoraphidium minutum
0.37
-
 ATP isozyme PGK1, pH 7.3 Monoraphidium minutum
0.37
-
 ATP ATP in form of MgATP2- Monoraphidium minutum
0.46
-
 3-phospho-D-glycerate isozyme PGK2, pH 7.3-7.8 Monoraphidium minutum
0.59
-
 3-phospho-D-glycerate isozyme PGK1, pH 7.3 Monoraphidium minutum

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ can partially replace Mg2+ in activation Monoraphidium minutum
Cd2+ can partially replace Mg2+ in activation Monoraphidium minutum
Co2+ can partially replace Mg2+ in activation Monoraphidium minutum
divalent cation descending order of activation potential Mg2+,Mn2+, Zn2+, Co2+, Cd2+, Ca2+, isozyme PGK1 is more activated than PGK2 Monoraphidium minutum
Mg2+ required Monoraphidium minutum
Mg2+ Mg2+ most efficient activator Monoraphidium minutum
Mg2+ above 10 mM inhibition of isozyme PGK1, not PGK2 Monoraphidium minutum
Mn2+ can partially replace Mg2+ in activation Monoraphidium minutum
Mn2+ more effective for isoenzyme PGK1 than for PGK2 Monoraphidium minutum
Zn2+ can partially replace Mg2+ in activation Monoraphidium minutum
Zn2+ more effective for isoenzyme PGK1 than for PGK2 Monoraphidium minutum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
44000
-
 isoenzyme PGK1 and PGK2, gel filtration Monoraphidium minutum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ADP + 3-phospho-D-glyceroyl phosphate Monoraphidium minutum energy charge is the most important factor in regulating the 2 forms of PGK ATP + 3-phospho-D-glycerate
-
 r

Organism

Organism UniProt Comment Textmining
Monoraphidium minutum
-
 2 isoforms PGK1 and PGK2, probably cytosolic and chloroplastic form
-

Purification (Commentary)

Purification (Comment) Organism
isozymes PGK-1, PGK-2, to homogeneity Monoraphidium minutum

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Monoraphidium minutum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + 3-phospho-D-glyceroyl phosphate energy charge is the most important factor in regulating the 2 forms of PGK Monoraphidium minutum ATP + 3-phospho-D-glycerate
-
 r
ATP + 3-phospho-D-glycerate
-
 Monoraphidium minutum ADP + 1,3-diphosphoglycerate
-
 r
ATP + 3-phospho-D-glycerate
-
 Monoraphidium minutum ADP + 3-phospho-D-glyceroyl phosphate
-
 r

Subunits

Subunits Comment Organism
monomer 1 * 44000, isoenzymes PGK1 and PGK2, SDS-PAGE Monoraphidium minutum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3
-
 PGK1 Monoraphidium minutum
7.3 7.8 PGK2 Monoraphidium minutum

Cofactor

Cofactor Comment Organism Structure
ADP
-
 Monoraphidium minutum
ATP required as phosphate donor Monoraphidium minutum