Editing Pyruvate kinase (section)

{{Short description|Class of enzymes}}
{{Infobox enzyme
| name = Pyruvate kinase
| image = Pyruvate kinase protein domains.png
| image_size = 
| caption = 3D structure of pyruvate kinase ({{PDBe-KB|1PKN}})
| EC_number = 2.7.1.40
| CAS_number = 9001-59-6
| GO_code = 0004743
}}
<!--  [[Image:pkb.jpg|thumb|right|250px|''Typical Pyruvate Kinase Structure, <small>X-ray [[Crystallography]] Derived</small>'']] -->
'''Pyruvate kinase''' is the [[enzyme]] involved in the last step of [[glycolysis]]. It [[catalyst|catalyzes]] the transfer of a [[phosphate group]] from [[phosphoenolpyruvate]] (PEP) to [[adenosine diphosphate]] (ADP), yielding one molecule of [[pyruvate]] and one molecule of [[adenosine triphosphate|ATP]].<ref>{{cite journal | vauthors = Gupta V, Bamezai RN | title = Human pyruvate kinase M2: a multifunctional protein | journal = Protein Science | volume = 19 | issue = 11 | pages = 2031–44 | date = November 2010 | pmid = 20857498 | pmc = 3005776 | doi = 10.1002/pro.505 }}</ref> Pyruvate kinase was inappropriately named (inconsistently with a conventional [[kinase]]) before it was recognized that it did not directly catalyze phosphorylation of [[pyruvate]], which does not occur under physiological conditions.<ref>{{cite book | vauthors = Goodman HM |title=Basic Medical Endocrinology |url=https://archive.org/details/basicmedicalendo00good_712 |url-access=limited |publisher=Elsevier |isbn=978-0-12-373975-9 |page=[https://archive.org/details/basicmedicalendo00good_712/page/n166 132] |edition=4th|year=2009 }}</ref> Pyruvate kinase is present in four distinct, tissue-specific isozymes in animals, each consisting of particular kinetic properties necessary to accommodate the variations in metabolic requirements of diverse tissues.