H
IPR015813

Pyruvate/Phosphoenolpyruvate kinase-like domain superfamily

InterPro entry
Short namePyrv/PenolPyrv_kinase-like_dom
Overlapping entries
 

Description

Pyruvate kinase controls the exit from the glysolysis pathway, catalysing the transfer of phosphate from phosphooenolpyruvate (PEP) to ADP. Mammalian pyruvate kinase is a homotetramer, where each polypeptide subunit consists of four domains: N-terminal, A domain, B domain and C-terminal. Activation of the enzyme is believed to occur via the clamping down of the B domain onto the A domain to dehydrate the active site cleft. The N- and C-terminal domains are situated at inter-subunit contact sites, and could be involved in assembly and communication within the complex. The N-terminal domain has a TIM β/α-barrel structure. Homologous TIM-barrel domains are found in the following proteins:


 * N-terminal of pyruvate kinase (
2.7.1.40
), which is interrupted by an all-beta domain
[1]
.
 * C-terminal of pyruvate phosphate dikinase (
2.7.9.1
), which has a similar mode of substrate binding to pyruvate kinase
[2]
.
 * Phosphoenolpyruvate carboxylase (
4.1.1.31
); this domain has additional helices
[3]
.
 * Phosphenolpyruvate mutase(
5.4.2.9
)/Isocitrate lyase (
4.1.3.1
), where it forms a swapped dimer
[4]
.
 * HpcH/HpaI aldolases, such as the beta subunit of citrate lyase, where it forms a swapped dimer, and contains a pyruvate kinase-type metal binding site
[5]
.
 * Ketopantoate hydroxymethyltransferase PanB (
2.1.2.11
), where a C-terminal helix exchange is observed in some enzymes
[6]
.

References

1.Structural and functional linkages between subunit interfaces in mammalian pyruvate kinase. Wooll JO, Friesen RH, White MA, Watowich SJ, Fox RO, Lee JC, Czerwinski EW. J. Mol. Biol. 312, 525-40, (2001). View articlePMID: 11563914

2.Pyruvate site of pyruvate phosphate dikinase: crystal structure of the enzyme-phosphonopyruvate complex, and mutant analysis. Herzberg O, Chen CC, Liu S, Tempczyk A, Howard A, Wei M, Ye D, Dunaway-Mariano D. Biochemistry 41, 780-7, (2002). View articlePMID: 11790099

3.Crystal structures of C4 form maize and quaternary complex of E. coli phosphoenolpyruvate carboxylases. Matsumura H, Xie Y, Shirakata S, Inoue T, Yoshinaga T, Ueno Y, Izui K, Kai Y. Structure 10, 1721-30, (2002). View articlePMID: 12467579

4.The structure and domain organization of Escherichia coli isocitrate lyase. Britton KL, Abeysinghe IS, Baker PJ, Barynin V, Diehl P, Langridge SJ, McFadden BA, Sedelnikova SE, Stillman TJ, Weeradechapon K, Rice DW. Acta Crystallogr. D Biol. Crystallogr. 57, 1209-18, (2001). View articlePMID: 11526312

5.Electron microscopic studies on retinochoroidal atrophy in the human eye. Okabe S, Matsuo N, Okamoto S, Kataoka H. Acta Med. Okayama 36, 11-21, (1982). PMID: 7064730

6.Structure of E. coli ketopantoate hydroxymethyl transferase complexed with ketopantoate and Mg2+, solved by locating 160 selenomethionine sites. von Delft F, Inoue T, Saldanha SA, Ottenhof HH, Schmitzberger F, Birch LM, Dhanaraj V, Witty M, Smith AG, Blundell TL, Abell C. Structure 11, 985-96, (2003). View articlePMID: 12906829

GO terms

biological process

  • None

cellular component

  • None

Cross References

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