Biomolecules and Enzymes

Ribozymes or RNA enzymes are catalytic RNA molecules. The first ribozyme discovered was self splicing group I intron. The second catalytic RNA was RNAase P which separates tRNA from hn RNA at their 5' ends. Peptidyl transferase involved in translation of proteins is also catalytic RNA. Telomerase is a ribonulceoprotein  enzyme. It is involved in replication of terminal DNA or telomeres.

Enzymes are biological catalysts which catalyse the biochemical reactions in living systems. Majority of enzymes are proteins. A small minority of enzymes are catalytic RNA molecules. These catalytic RNA molecules are called ribozymes. These catalytic RNA molecules catalyze reactions like splicing of introns during processing of RNA in eukaryotic mRNA.

Co-enzymes tightly or covalently bonded to enzymes are called prosthetic groups, e.g., pyridoxal phosphate, heme, biotin. Heme is a prosthetic group containing ferrous ion. It is important for a number of biologically important hemoproteins such as myoglobin, cytochrome oxidase, catalase and peroxidase. Thus, the correct answer is option E.

Some enzymes require metal ions for their activity. Tyrosinase is a copper containing enzyme that catalyzes the production of melanin and other pigments.

Simple enzymes consist of only proteins and catalyze their substrate specific reactions. Urease is an enzyme which is only made up of protein and it functions to catalyze the hydrolysis of urea which results in the formation of ammonia and carbon dioxide.

Hydrolase is a class of enzyme which act as biochemical catalysts that use water to break chemical bonds.

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.

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.

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.

Enzymes are biocatalyst that affects the rate of biochemical reactions they generally have the same pH and temperature Optima at which they work efficiently. 

Enzymes are simple if they are made up of only proteins, e.g., pepsin, amylase, etc., while conjugate enzymes have an additional non-protein cofactor, e.g., dehydrogenase enzymes. The cofactor can be organic or inorganic. Loosely attached organic cofactor are called coenzymes, e.g., NAD, FAD etc., while firmly attached one is prosthetic group, e.g., haeme, biotin etc.