Pyruvate/Phosphoenolpyruvate kinase-like domain superfamily
Short name | Pyrv/PenolPyrv_kinase-like_dom |
Overlapping entries |
Description
* N-terminal of pyruvate kinase (
* C-terminal of pyruvate phosphate dikinase (
* Phosphoenolpyruvate carboxylase (
* Phosphenolpyruvate mutase(
* 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
* Ketopantoate hydroxymethyltransferase PanB (
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
Cross References
Contributing Member Database Entry
- SUPERFAMILY:SSF51621