Tag: enzymes

The EC number 4.2.1.7 is assigned to the enzyme named altronate dehydratase or D-altronate hydro-lyase. This enzyme catalyses the dehydration of D-altronate and results in the formation of 2-dehydroxy-3-deoxy-D-gluconate and water. 

Phosphodiesterase is a hydrolase enzyme. So, it's EC number is 3.

Natural source of subtilin is bacteria Bacillus subtilis. Subtilisins are proteolytic enzymes mainly used in detergents and house hold cleaning products to remove proteinaceous deposits and stains.

Histone proteins are rich in basic amino acids and form the core around which the DNA is wound giving rise to nucleosome particles. DNA is wound around histones because basic amino acids are positively charged at physiological pH which facilitates winding of acidic or negatively charged DNA. Neutralization of positive charge, on basic amino acids of histone proteins, by chemical processes like reversible acetylation will lead to neutralization of attractive force between nucleosome core and DNA molecule. This will in turn lead to transcriptional activation (histone proteins are acetylated) and after transcription once again the histone proteins will be deacetylated restoring there positive charge, thus facilitating the tight binding between (negatively charged) DNA and (positively charged) histone core. Apart from reversible acetylation, histone proteins also undergo a number of other chemical modifications. Thus, acting as modulators for DNA metabolism.

in 1897, Eduard Buchner discovered that yeast extracts could ferment sugar to alcohol, proving that fermentation was promoted by molecules that continued to function when removed from cells. Frederick W. Khne called these molecules as enzymes. The isolation and crystallization of urease by James Sumner, in 1926, provided a breakthrough in early enzyme studies. Sumner found that urease crystals consisted entirely of protein, and he postulated that all enzymes are proteins. In the absence of other examples, this idea remained controversial for some time. Only in the 1930s, was Sumners conclusion widely accepted, after John Northrop and Moses Kunitz crystallized pepsin, trypsin, and other digestive enzymes and found them also to be proteins.

Isoenzymes are an unique example in which the same reaction may be catalyzed by two or more different molecular forms of an enzyme. The multiple forms, called isozymes or isoenzymes, may occur in the same species, in the same tissue, or even in the same cell. The different forms of the enzyme generally differ in kinetic or regulatory properties, in the cofactor they use (NADH or NADPH for dehydrogenase isozymes, for example), or in their subcellular distribution (soluble or membrane-bound). Isozymes may have similar, but not identical, amino acid sequences, and in many cases they clearly share a common evolutionary origin. One of the first enzymes found to have isozymes was lactate dehydrogenase (LDH), which, in vertebrate tissues, exists as at least five different isozymes separable by electrophoresis. However, isoenzymes follow the same general mechanism of enzyme action, i.e., decreasing the activation energy of substrates for a reaction.

Gastrin is a peptide hormone, which is secreted by the gastric glands in the stomach wall. The gastrin stimulates secretion of gastric juice rich in pepsin and hydrochloric acid. The stimulation for secretion of gastrin is presence of peptides derived from dietary proteins.

Enzymes are biological catalysts. The multitude of biochemical reactions that make cellular metabolism possible are due to enzymes. The isolation and crystallization of urease by James Sumner in 1926 provided a breakthrough in early enzyme studies. Sumner found that urease crystals consisted entirely of protein, and he postulated that all enzymes are proteins. In the absence of other examples, this idea remained controversial for some time. Only in the1930s, was Sumners conclusion widely accepted, after John Northrop and Moses Kunitz crystallized pepsin, trypsin, and other digestive enzymes and found them also to be proteins.

An amylase is an enzyme that catalyses the hydrolysis of starch into sugars. A hydrolase or hydrolytic enzyme is an enzyme that catalyzes the hydrolysis of a chemical bond. So, the correct answer is option C.

The non-protein component or prosthetic group along with the protein component or apoenzyme is called the holoenzyme. The prosthetic group may be metal ion or a co-enzyme that may be firmly or losely bound to the enzyme.
So, the correct answer is option B.