Protein Family Models

Pyruvate kinase catalyses the final step in glycolysis, the conversion of phosphoenolpyruvate to pyruvate with concomitant phosphorylation of ADP to ATP [1,2]. The structure of several pyruvate kinases from various organisms have been determined [2, 3,4]. The protein comprises three-four domains: a small N-terminal helical domain (absent in bacterial PK), a beta/alpha barrel domain, a beta-barrel domain (inserted within the beta/alpha-barrel domain), and a 3-layer alpha/beta/alpha sandwich domain (represented in this entry). This domain is at the C-terminal of pyruvate kinases and contains the FBP (fructose 1,6-bisphosphate) binding site [2,4,5]. [1]. 9308890. Ligand-induced domain movement in pyruvate kinase: structure of the enzyme from rabbit muscle with Mg2+, K+, and L-phospholactate at 2.7 A resolution. Larsen TM, Benning MM, Wesenberg GE, Rayment I, Reed GH;. Arch Biochem Biophys 1997;345:199-206. [2]. 10751408. The allosteric regulation of pyruvate kinase. Valentini G, Chiarelli L, Fortin R, Speranza ML, Galizzi A, Mattevi A;. J Biol Chem. 2000;275:18145-18152. [3]. 12798932. Pyruvate kinase: current status of regulatory and functional properties. Munoz ME, Ponce E;. Comp Biochem Physiol B Biochem Mol Biol. 2003;135:197-218. [4]. 11960989. Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia. Valentini G, Chiarelli LR, Fortin R, Dolzan M, Galizzi A, Abraham DJ, Wang C, Bianchi P, Zanella A, Mattevi A;. J Biol Chem. 2002;277:23807-23814. [5]. 29748232. An allostatic mechanism for M2 pyruvate kinase as an amino-acid sensor. Yuan M, McNae IW, Chen Y, Blackburn . TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

This is the barrel domain of pyruvate kinases. This domain represents the beta/alpha barrel and the small beta-barrel domain inserted within it. The active site is found in a cleft between the two domains [1,2,3,4]. [1]. 9308890. Ligand-induced domain movement in pyruvate kinase: structure of the enzyme from rabbit muscle with Mg2+, K+, and L-phospholactate at 2.7 A resolution. Larsen TM, Benning MM, Wesenberg GE, Rayment I, Reed GH;. Arch Biochem Biophys 1997;345:199-206. [2]. 12798932. Pyruvate kinase: current status of regulatory and functional properties. Munoz ME, Ponce E;. Comp Biochem Physiol B Biochem Mol Biol. 2003;135:197-218. [3]. 11960989. Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia. Valentini G, Chiarelli LR, Fortin R, Dolzan M, Galizzi A, Abraham DJ, Wang C, Bianchi P, Zanella A, Mattevi A;. J Biol Chem. 2002;277:23807-23814. [4]. 29748232. An allostatic mechanism for M2 pyruvate kinase as an amino-acid sensor. Yuan M, McNae IW, Chen Y, Blackburn EA, Wear MA, Michels PAM, Fothergill-Gilmore LA, Hupp T, Walkinshaw MD;. Biochem J. 2018;475:1821-1837. (from Pfam)

Date:

2024-10-16

Catalyzes the formation of phosphoenolpyruvate from pyruvate

Date:

2020-10-26

Catalyzes the formation of phosphoenolpyruvate from pyruvate

Gene:

pykF

Date:

2021-10-15

pyruvate kinase PykF catalyzes the phosphorylation of pyruvate to form phosphoenolpyruvate and functions in regulating glycolysis

Date:

2019-06-13

This enzyme is a homotetramer. Some forms are active only in the presence of fructose-1,6-bisphosphate or similar phosphorylated sugars.

Gene:

pyk

Date:

2024-11-07

Catalyzes the formation of phosphoenolpyruvate from pyruvate

Date:

2020-10-26