4.2.1.11	2,3-diketo-5-methylthiopentane 1-phosphate	methionine salvage pathway	
4.2.1.11	2,3-dioxo-5-methylthio-1-phosphopentane + 4 H+	-	
4.2.1.11	2-phospho-D-glycerate	-	
4.2.1.11	2-phospho-D-glycerate	age-related changes in the properties of the enzyme	
4.2.1.11	2-phospho-D-glycerate	enzyme of glycolysis	
4.2.1.11	2-phospho-D-glycerate	beta,beta-enolase binds with high affinity the adjacent enzymes in the glycolytic pathway (pyruvate kinase and phosphoglycerate mutase), beta,beta-enolase binds with high affinity sarcomeric troponin but not actin and tropomyosin	
4.2.1.11	2-phospho-D-glycerate	the enzyme is a plasminogen binding protein	
4.2.1.11	2-phospho-D-glycerate	analysis of pathogenesis of Streptococcus suis: rSsEno binds to fibronectin and plasminogen	
4.2.1.11	2-phospho-D-glycerate	the enzyme is involved in the modified Embden-Meyerhof pathway	
4.2.1.11	2-phospho-D-glycerate	the enzyme probably functions in sugar fermentation pathway	
4.2.1.11	additional information	enolase acts as a DNA methyltransferase 2 inhibitor. Enolase interacts with Ehmeth, and modulates its activity under conditions of glucose starvation inhibiting the binding of Ehmeth and human DNA methyltransferase 2 to Entamoeba histolytica MRS2 DNA	
4.2.1.11	additional information	ENOA has C-terminal lysines predominantly responsible for plasminogen activation, interaction of the plasminogen lysinebinding sites with ENOA is dependent upon recognition of ENOA C-terminal lysines K420, K422 and K434, and also K256	
4.2.1.11	additional information	enolase shows plasminogen-binding activity	
4.2.1.11	additional information	plasminogen bound to recombinant enolase can be converted to active plasmin	
4.2.1.11	phosphoenolpyruvate + H2O	analysis of pathogenesis of Bacillus anthracis: binding of human plasminogen and laminin