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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Enzyme: cytosolic 3-phosphoglycerate kinase

Synonyms: 3-PGKc, cytosolic 3-phosphoglycerate kinase

Species: Spinacia oleracea

Summary:
A protein with 3-phoshoglycerate kinase activity was purified from a crude extract of spinach (Spinacia oleracea L.). In fact two isoforms of the protein were identified through this procedure: one is cytosolic (this protein), the other chloroplastic (see plastidic 3-phosphoglycerate kinase). The chloroplastic protein was also purified from isolated chloroplasts, allowing the exact determination of the identity of each crude extract-purified isoform [KopkeSecundo90]. The cytosolic protein has a molecular weight of 39 kDa by size exclusion chromatography (40.7 kDa on SDS-PAGE). The protein is monomeric. Its pH optimum is at 7.5 with a strong drop of activity at higher and lower pH values [KopkeSecundo90].

Locations: cytosol

Molecular Weight of Polypeptide: 39 kD (experimental) [KopkeSecundo90 ]

Gene-Reaction Schematic: ?

GO Terms:

Cellular Component: GO:0005829 - cytosol [KopkeSecundo90]

Credits:
Created 09-Nov-2006 by Tissier C , TAIR


Enzymatic reaction of: 3-phosphoglycerate kinase

EC Number: 2.7.2.3

3-phospho-D-glycerate + ATP <=> 1,3-bisphospho-D-glycerate + ADP

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

This reaction is reversible.

In Pathways: superpathway of cytosolic glycolysis (plants), pyruvate dehydrogenase and TCA cycle , superpathway of anaerobic sucrose degradation , glycolysis IV (plant cytosol) , sucrose biosynthesis I (from photosynthesis)

Summary:
The protein does not follow Michaelis-Menten kinetics for this reaction. The kinetics are biphasic and the enzyme exhibits 4-6 times higher affinity for the substrate in the lower concentration range than in the higher range [KopkeSecundo90].

Low concentration range: Km (MgATP) 240 μM, Km (3-PGA) 280 μM.

High concentration range: Km (MgATP) 1460 μM, Km (3-PGA) 1220 μM.

Inhibitors (Other): ATP [KopkeSecundo90]

Primary Physiological Regulators of Enzyme Activity: ATP

Kinetic Parameters:

Substrate
Km (μM)
Citations
ATP
240.0
[KopkeSecundo90]
3-phospho-D-glycerate
280.0
[KopkeSecundo90]

pH(opt): 7.5 [KopkeSecundo90]


References

KopkeSecundo90: Kopke-Secundo E., Molnar I., Schnarrenberger C. (1990). "Isolation and characterization of the cytosolic and chloroplastic 3-phosphoglycerate kinase from spinach leaves." Plant Physiol. 93:40-47.


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Thu Dec 18, 2014, biocyc14.