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In biochemistry, isozymes (also known as isoenzymes or more generally as multiple forms of enzymes) are enzymes that differ in amino acid sequence but catalyze the same chemical reaction. Isozymes usually have different kinetic parameters (e.g. different K M values), or are regulated differently.
Properties. Allosteric enzymes are generally larger in mass than other enzymes. Different from having a single subunit enzyme, in this case they are composed of multiple subunits, which contain active sites and regulatory molecule binding sites. They present a special kinetics: the cooperation. In here, configuration changes in each chain of ...
The hydroxylated metabolite, that also has weak COX-2-specific inhibitory properties, is then further metabolized by non-cytochrome P450 pathway to a glucuronide metabolite. These metabolites are excreted in the urine. [17] After intra-muscular administration of Parecoxib sodium peak plasma concentration is reached within 15 minutes.
Hexokinases I, II, and III are referred to as low-K m isoenzymes because of a high affinity for glucose (below 1 mM). Hexokinases I and II follow Michaelis-Menten kinetics at physiological concentrations of substrates. [citation needed] All three are strongly inhibited by their product, glucose-6-phosphate. Molecular masses are around 100 kDa ...
As a result, the kinetic and regulatory properties of the various isoenzymes pools are dependent on subunit composition. Tissue-specific changes in PFK activity and isoenzymic content contribute significantly to the diversities of glycolytic and gluconeogenic rates which have been observed for different tissues.
Enolase 1 (ENO1), more commonly known as alpha-enolase, is a glycolytic enzyme expressed in most tissues, one of the isozymes of enolase.Each isoenzyme is a homodimer composed of 2 alpha, 2 gamma, or 2 beta subunits, and functions as a glycolytic enzyme.
Reaction catalyzed by lactate dehydrogenase. Lactate dehydrogenase catalyzes the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD +.It converts pyruvate, the final product of glycolysis, to lactate when oxygen is absent or in short supply, and it performs the reverse reaction during the Cori cycle in the liver.
Enolase is a member of the large enolase superfamily.It has a molecular weight of 82,000–100,000 daltons depending on the isoform. [3] [4] In human alpha enolase, the two subunits are antiparallel in orientation so that Glu 20 of one subunit forms an ionic bond with Arg 414 of the other subunit. [3]