ABSTRACT a-Enolase is an important glycolytic enzyme in the cytoplasm of prokaryotic and eukaryotic cells and is considered a multifunctional protein
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ABSTRACT a-Enolase is an important glycolytic enzyme in the cytoplasm of prokaryotic and eukaryotic cells and is considered a multifunctional protein. a-Enolase is expressed on several cell surface, where it acts as a plasminogen receptor, hydrolyzing the inactive plasminogen into active proteolytic plasmin. In addition to glycolytic enzyme and plasminogen receptor functions, a-Enolaseperforms other cellular functions and found at varying subcellular localizations that are distinct from its well-established function in glycolysis. Therapeutically a-enolase is an essential enzyme as many streptococcal species such as Streptococcus mutansuses plasminogen binding site of a- enolase to spread infective endocarditis. In this study functional identity of recombinant a-enolase has been confirmed by its ability to catalyze glycolytic reactions and its enzyme kinetics.a-Enolase is localized on the surface of hematopoietic cells such as monocytes, T cells and B cells, neuronal cells, and endothelial cells as a strong plasminogen receptor, modulating pericellularfibrinolytic activity. Table of content TOPIC PAGE NO. ABSTRACT 1 INTRODUCTION 3 METHOD 6 DISCUSSION 14 REFERENCES 15 INTRODUCTION Enolase (2-phospho-D-glycerate hydrolyase, EC4.2.1.11) is a key glycolytic enzyme [1] in the cytotoplasma of both prokaryotes and eukaryotes and is also considered as multifunctional protein. It is also one of the most abundantly expressed cytosolic enzyme in many organisms discovered in 1934 by Lohman and Mayerhof. Itcatalyzes the dehydration of 2-phospho D-glycerate (2PGA) to phosphoenolpyruvate (PEP) in glycolysis as shown in figure 2, and the reverse reaction in gluconeogenesis.Before binding with substrate enolase form complex with divalent metal cations and hence it is characterize as metalloenzyme. It shows highest activity when bound to metallic cation…
ABSTRACT a-Enolase is an important glycolytic enzyme in the cytoplasm of prokaryotic and eukaryotic cells and is considered a multifunctional protein. a-Enolase is expressed on several cell surface, where it acts as a plasminogen receptor, hydrolyzing the inactive plasminogen into active proteolytic plasmin. In addition to glycolytic enzyme and plasminogen receptor functions, a-Enolaseperforms other cellular functions and found at varying subcellular localizations that are distinct from its well-established function in glycolysis. Therapeutically a-enolase is an essential enzyme as many streptococcal species such as Streptococcus mutansuses plasminogen binding site of a- enolase to spread infective endocarditis. In this study functional identity of recombinant a-enolase has been confirmed by its ability to catalyze glycolytic reactions and its enzyme kinetics.a-Enolase is localized on the surface of hematopoietic cells such as monocytes, T cells and B cells, neuronal cells, and endothelial cells as a strong plasminogen receptor, modulating pericellularfibrinolytic activity. Table of content TOPIC PAGE NO. ABSTRACT 1 INTRODUCTION 3 METHOD 6 DISCUSSION 14 REFERENCES 15 INTRODUCTION Enolase (2-phospho-D-glycerate hydrolyase, EC4.2.1.11) is a key glycolytic enzyme [1] in the cytotoplasma of both prokaryotes and eukaryotes and is also considered as multifunctional protein. It is also one of the most abundantly expressed cytosolic enzyme in many organisms discovered in 1934 by Lohman and Mayerhof. Itcatalyzes the dehydration of 2-phospho D-glycerate (2PGA) to phosphoenolpyruvate (PEP) in glycolysis as shown in figure 2, and the reverse reaction in gluconeogenesis.Before binding with substrate enolase form complex with divalent metal cations and hence it is characterize as metalloenzyme. It shows highest activity when bound to metallic cation…
