Prosthetic group glycoprotein

Biosynthesis of the polypeptide chain is realised by a complicated process called translation. The basic polypeptide chain is subsequently chemically modified by the so-called posttranslational modifications. During this sequence of events the peptide chain can be cleaved by directed proteolysis, some of the amino acids can be covalently modified (hydroxylated, dehydrogenated, amidated, etc.) or different so-called prosthetic groups such as haem (haemoproteins), phosphate residues (phosphoproteins), metal ions (metal-loproteins) or (oligo)saccharide chains (glycoproteins) can be attached to the molecule by covalent bonds. Naturally, one protein molecule can be modified by more means. 

The second ligninolytic enzyme, MnP, has been identified (U), purified and characterized (13-16). MnP is an H O -dependent heme glycoprotein (M -46,000) with an iron protoporphyrin iX prosthetic group. MnP catalyzes the Mn -dependent oxidation of a variety of phenols and phenolic lignin model compounds (6,8.13-15,17). Electronic absorption... 

Proteins with molecular weights in the millions are the major constituents of all living cells. Simple proteins are hydrolyzed only to amino acids. Coqjugated proteins are hydrolyzed to amino acids and nonpeptide substances known as prosthetic groups. These prosthetic groups include nucleic acids of nucieoproteins, carbohydrates of glycoproteins, pigments (such as hemin and chiorophyli) of chromoproteins, and fats or lipids of lipoproteins. 

One of the cellobiose oxidoreductases present in S. pulverulentum has been characterised and named cellobiose oxidase (Ander and Eriksson, 1978). The enzyme contains both haem and flavin co factors and binds irreversibly to concanavalin A-Sepharose, suggesting that it is a glycoprotein. Cellobiose oxidase from S. pulverulentum has now been purified to homogeneity by Morpeth (1985). The carbohydrate and amino acid compositions of the enzyme have been determined. The enzyme contains FAD and cytochrome b prosthetic groups and is a monomer with an Mr of 74400 determined by sedimentation equilibrium. 

Some proteins also contain other compounds, apart from amino acids. These proteins are known as conjugated proteins and the non-amino acid part is known as a prosthetic group (Chap. 8) the protein part is termed the apoprotein. Glycoproteins (Chap. 6) and proteoglycans (Chap. 5) contain covalently bound carbohydrate, while lipoproteins (Chap. 6) contain lipid as the prosthetic groups. 

An enzyme may be a protein or a glycoprotein, and consists of at least one polypeptide moiety. The regions of the enzyme that are directly involved in the catalytic process are called the active sites. An enzyme may have one or more groups that are essential for catalytic activity associated with the active sites through either covalent or noncovalent bonds the protein or glycoprotein moiety in such an enzyme is called the apoenzyme, while the nonprotein moiety is called the prosthetic group. The combination of the apoenzyme with the prosthetic group yields the holoenzyme. 

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