Enzyme enolase catalyzes the conversion of two PGA to phosphoenol acid within the presence of a cofactor
a) ${Mn}^{2+}$
b) ${Fe}^{2+}$
c) ${ Mg }^{ 2+ }$
d) ${Zn}^{2+}$
Answer
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Hint: The breakdown of glucose molecules generates two net ATP (ATP) molecules, which provides a readily available source of energy for various reactions within the cell, and two pyruvate molecules, which may be further converted into lactate (used in gluconeogenesis), acetyl-CoA (used in the acid cycle), oxaloacetate (used in the acid cycle), and alanine (used in transmission reactions) .
Complete answer
Enolase , also called phosphopyruvate hydratase, is an enzyme that catalyzes a reaction of glycolysis.
The glycolysis process converts glucose into two 3-carbon molecules called pyruvate. Enolase is used to convert 2-phosphoglycerate (2PG) to phosphoenolpyruvate (PEP) within the 9th reaction of glycolysis.
The reaction catalyzed by enolase :
${ 2-phospho-D-glycerate phosphor enolpyruvate\quad +\quad { H }_{ 2 }{ O } }$
This enzyme requires ${ Mg }^{ 2+ }$ for catalysis and will even be activated by other divalent cations where ${ Mg }^{ 2+ }$ gives absolutely the best activity. Enolase is expressed abundantly in most cells and has been proven useful as a model to review mechanisms of enzyme action and structural analysis.
So the correct answer is' '${ Mg }^{ 2+ }$’.
Additional information: The secondary structure of enolase contains both alpha helices and beta sheets. The beta-sheets are mainly enolase and have about 36 alpha helices and 22 beta sheets (18 alpha helices and 11 beta-sheets per domain) . Enolase consists of two domains.
Structural Classification of Proteins (SCOP): Enolase is within the alpha and beta proteins class and features a fold of TIM beta/alpha-barrel. It comes from the Superfamily on Enolase C-terminal domain-like and is within the enolase family.
In many organisms like vertebrates, brewer's yeast, Toxoplasma gondii the presence of varied enolase isoforms has been reported by performing studies, often with kinetic properties favoring a flux within the glycolytic or gluconeogenic direction. Invertebrates, it's been shown that expression of the numerous enolase isoforms, formed by homodimers and heterodimers of α, β, and γ subunits, is regulated during a developmentally and/or tissue-specific manner.
Note: Enolase is present altogether tissues and organisms with the facility to undertake glycolysis or fermentation. Recent studies have illustrated that the Enolase concentration samples so on compute certain conditions and their severity. allow us to take an example of the high concentrations of Enolase in the spinal fluid (CSF) that are more strongly related to astrocytoma than other enzymes like aldolase, pyruvate kinase, and creatine kinase.
Complete answer
Enolase , also called phosphopyruvate hydratase, is an enzyme that catalyzes a reaction of glycolysis.
The glycolysis process converts glucose into two 3-carbon molecules called pyruvate. Enolase is used to convert 2-phosphoglycerate (2PG) to phosphoenolpyruvate (PEP) within the 9th reaction of glycolysis.
The reaction catalyzed by enolase :
${ 2-phospho-D-glycerate phosphor enolpyruvate\quad +\quad { H }_{ 2 }{ O } }$
This enzyme requires ${ Mg }^{ 2+ }$ for catalysis and will even be activated by other divalent cations where ${ Mg }^{ 2+ }$ gives absolutely the best activity. Enolase is expressed abundantly in most cells and has been proven useful as a model to review mechanisms of enzyme action and structural analysis.
So the correct answer is' '${ Mg }^{ 2+ }$’.
Additional information: The secondary structure of enolase contains both alpha helices and beta sheets. The beta-sheets are mainly enolase and have about 36 alpha helices and 22 beta sheets (18 alpha helices and 11 beta-sheets per domain) . Enolase consists of two domains.
Structural Classification of Proteins (SCOP): Enolase is within the alpha and beta proteins class and features a fold of TIM beta/alpha-barrel. It comes from the Superfamily on Enolase C-terminal domain-like and is within the enolase family.
In many organisms like vertebrates, brewer's yeast, Toxoplasma gondii the presence of varied enolase isoforms has been reported by performing studies, often with kinetic properties favoring a flux within the glycolytic or gluconeogenic direction. Invertebrates, it's been shown that expression of the numerous enolase isoforms, formed by homodimers and heterodimers of α, β, and γ subunits, is regulated during a developmentally and/or tissue-specific manner.
Note: Enolase is present altogether tissues and organisms with the facility to undertake glycolysis or fermentation. Recent studies have illustrated that the Enolase concentration samples so on compute certain conditions and their severity. allow us to take an example of the high concentrations of Enolase in the spinal fluid (CSF) that are more strongly related to astrocytoma than other enzymes like aldolase, pyruvate kinase, and creatine kinase.
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