Literature summary for 4.2.1.11 extracted from

Carmieli, R.; Larsen, T.M.; Reed, G.H.; Zein, S.; Neese, F.; Goldfarb, D.
The catalytic Mn2+ sites in the enolase-inhibitor complex: crystallography, single-crystal EPR, and DFT calculations (2007), J. Am. Chem. Soc., 129, 4240-4252.

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of enolase-Zn2+/Mn2+ complex formation with phosphonoacetohydroxamate solved to 1.54 A resolution by X-ray crystallography, replacement of native Mg2+ ions with Mn2+/Zn2+ introduces only minor atom displacements in the binding site, crystallographic data refined, simulations reveal a model of the enolase active site chosen for the study indicating sites MI and MII either occupied with Mn2+ at site MI and Zn2+ at site MII or vice versa, stereo view of the coordination of the two metal ions in the enolase-inhibitor-complex and of key active site residues presented, rotation patterns shown	Saccharomyces cerevisiae

Crystallization (Comment)

Organism

structure of enolase-Zn2+/Mn2+ complex formation with phosphonoacetohydroxamate solved to 1.54 A resolution by X-ray crystallography, replacement of native Mg2+ ions with Mn2+/Zn2+ introduces only minor atom displacements in the binding site, crystallographic data refined, simulations reveal a model of the enolase active site chosen for the study indicating sites MI and MII either occupied with Mn2+ at site MI and Zn2+ at site MII or vice versa, stereo view of the coordination of the two metal ions in the enolase-inhibitor-complex and of key active site residues presented, rotation patterns shown

Saccharomyces cerevisiae

Inhibitors

Inhibitors	Comment	Organism	Structure
phosphonoacetohydroxamate	preference for formation of hybrid Zn2+/Mn2+ complexes with enolase, in vitro activity of the complexed enolase in presence of phosphonoacetohydroxamate investigated by crystallography and electron paramagnetic resonance spectroscopy	Saccharomyces cerevisiae

Metals/Ions

Metals/Ions	Comment	Organism
Mg2+	activity depends on	Saccharomyces cerevisiae
Mn2+	catalytic binding sites analyzed in vitro	Saccharomyces cerevisiae
Zn2+	catalytic binding sites analyzed in vitro	Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
2-phospho-D-glycerate	Saccharomyces cerevisiae	-	phosphoenolpyruvate + H2O	-	r

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	P00924	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2-phospho-D-glycerate	-	Saccharomyces cerevisiae	phosphoenolpyruvate + H2O	-	r
2-phospho-D-glycerate	in vitro studies on catalytic, divalent cation binding sites	Saccharomyces cerevisiae	phosphoenolpyruvate + H2O	-	r

Synonyms

Synonyms	Comment	Organism
enolase	-	Saccharomyces cerevisiae