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Literature summary for 2.7.2.3 extracted from

  • Bowler, M.W.
    Conformational dynamics in phosphoglycerate kinase, an open and shut case? (2013), FEBS Lett., 587, 1878-1883.
    View publication on PubMed
Search for more literature for 2.7.2.3

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + 3-phospho-D-glycerate Homo sapiens
-
 ADP + 3-phospho-D-glyceroyl phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate catalytic mechanism and cycle, conformational changes for substrate binding and positioning, overview Homo sapiens
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 3-phospho-D-glycerate
-
 Homo sapiens ADP + 3-phospho-D-glyceroyl phosphate
-
 ?

Synonyms

Synonyms Comment Organism
PGK
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Homo sapiens

General Information

General Information Comment Organism
additional information Brownian forces acting on the protein are the dominant factor in the catalytic cycle, the enzyme has evolved measures to harness this force for efficient catalysis. PGK is composed of two domains with the 3-phospho-D-glycerate or 3-phospho-D-glyceroyl phosphate binding site in the N-domain and the nucleotide binding site in the C-domain. In the absence of substrates, the enzyme is in an open conformation in which the two sites are separated and exposed to the solvent for rapid substrate/product exchange. In order for catalysis to occur, hinge bending leads to a closed conformation that results the formation of the active site and the correct placement of the substrates for nucleophilic attack. Structure of open and closed enzyme conformation, modelling, overview Homo sapiens
physiological function PGK is the enzyme responsible for the first ATP generating step of glycolysis, The enzyme implicated in oncogenesis and the in vivo activation of L-nucleoside pro-drugs effective against retroviruses. Its mechanism requires considerable hinge bending to bring the substrates into proximity in order for phosphoryl transfer to occur. PGK activity is used as a signalling mechanism in oncogenesis, where it displays activity as a disulphide reductase Homo sapiens