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Literature summary for 2.7.1.40 extracted from

  • Li, F.; Yu, T.; Zhao, Y.; Yu, S.
    Probing the catalytic allosteric mechanism of rabbit muscle pyruvate kinase by tryptophan fluorescence quenching (2012), Eur. Biophys. J., 41, 607-614.
    View publication on PubMed
Search for more literature for 2.7.1.40

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli strain BL21 Oryctolagus cuniculus

Protein Variants

Protein Variants Comment Organism
W157A site-directed mutagenesis, Trp157 is located in domain B and close to the active site Oryctolagus cuniculus
W481A/W514A site-directed mutagenesis, Trp481 and Trp514 are located in domain C and close to the Y-interface Oryctolagus cuniculus

Inhibitors

Inhibitors Comment Organism Structure
additional information interactions with Mg2+ and K+ lead to more exposed tryptophan residues of PK while interactions with phosphoenolpyruvate and ADP decrease solvent accessibility of the tryptophan residues Oryctolagus cuniculus
phenylalanine allosteric inhibitor Oryctolagus cuniculus

Metals/Ions

Metals/Ions Comment Organism Structure
K+ K+ is directly involved in the acquisition of the active conformation and movement of the B domain of the enzyme Oryctolagus cuniculus
Mg2+ required Oryctolagus cuniculus
additional information interaction of three Trp residues, Tr157, Trp481, and Trp514, with activating cations, overview. The majority of changes in tryptophan fluorescence signal from PK induced by the binding of activating cations come from Trp157. Interactions with Mg2+ and K+ lead to more exposed tryptophan residues of PK while interactions with phosphoenolpyruvate and ADP decrease solvent accessibility of the tryptophan residues Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + pyruvate Oryctolagus cuniculus
-
 ADP + phosphoenolpyruvate
-
 r

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes in Escherichia coli strain BL21 Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
muscle
-
 Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + pyruvate
-
 Oryctolagus cuniculus ADP + phosphoenolpyruvate
-
 r

Subunits

Subunits Comment Organism
homotetramer structure of muscle isozyme homotetramer and of the four monomers with Y-interface and Z-interface, each monomer consists of the N-terminal domain, domain A, domain B, and domain C, overview Oryctolagus cuniculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
23
-
 assay at Oryctolagus cuniculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Oryctolagus cuniculus

Cofactor

Cofactor Comment Organism Structure
ADP
-
 Oryctolagus cuniculus
ATP
-
 Oryctolagus cuniculus

General Information

General Information Comment Organism
additional information movement of the B domain is essential for the catalytic reaction. Rotation of the B domain in the opening of the cleft between domains B and A induced by the binding of activating cations allows substrates to bind, whereas substrate binding shifts the rotation of the B domain in the closure of the cleft. The enzyme exhibits a more dynamic structure after binding of activating metal ions and substrates, whereas binding of Phe decreases the dynamics Oryctolagus cuniculus
physiological function catalytic allosteric mechanism, overview Oryctolagus cuniculus