Biomaterial Database

[The effect of Maillard reaction products on enzyme reactions]. 1996

D Schumacher, and L W Kroh

Institut für Lebensmittelchemie, Technischen Universität Berlin.

In this article current knowledge about the Maillard reaction in vivo is described first, especially the glycosylation reactions of various tissues and the identification of different final products and intermediates of Maillard reaction. The influence of MRP on digestion is of significant importance. These products are absorbed in different ways and are excreted in various amounts. Hence, the organism is variably influenced by MRP. The influence of defined MRP, of glycosylated proteins and of melanoidins on glycosidases and proteases is described. The effects produced depend on the enzyme and on the used MRP. Reactive alpha-dicarbonyl compounds play an important role in the organism. Further possible reactions of these compounds caused by reductases are discussed. The protein structure of enzymes is changed by Maillard reaction. Thereby the enzyme activity is influenced by covalent modifications of different amino acids and by inter- and intramolecular crosslinking. Finally, the use of enzymes and monoclonal antibodies for detection of MRP is discussed.

UI	MeSH Term	Description	Entries
D010088	Oxidoreductases	The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)	Dehydrogenases,Oxidases,Oxidoreductase,Reductases,Dehydrogenase,Oxidase,Reductase
D010450	Endopeptidases	A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.	Endopeptidase,Peptide Peptidohydrolases
D011108	Polymers	Compounds formed by the joining of smaller, usually repeating, units linked by covalent bonds. These compounds often form large macromolecules (e.g., BIOPOLYMERS; PLASTICS).	Polymer
D011487	Protein Conformation	The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).	Conformation, Protein,Conformations, Protein,Protein Conformations
D011506	Proteins	Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.	Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene
D006026	Glycoside Hydrolases	Any member of the class of enzymes that catalyze the cleavage of the glycosidic linkage of glycosides and the addition of water to the resulting molecules.	Endoglycosidase,Exoglycosidase,Glycohydrolase,Glycosidase,Glycosidases,Glycoside Hydrolase,Endoglycosidases,Exoglycosidases,Glycohydrolases,Hydrolase, Glycoside,Hydrolases, Glycoside
D006031	Glycosylation	The synthetic chemistry reaction or enzymatic reaction of adding carbohydrate or glycosyl groups. GLYCOSYLTRANSFERASES carry out the enzymatic glycosylation reactions. The spontaneous, non-enzymatic attachment of reducing sugars to free amino groups in proteins, lipids, or nucleic acids is called GLYCATION (see MAILLARD REACTION).	Protein Glycosylation,Glycosylation, Protein
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D015416	Maillard Reaction	A group of nonenzymatic reactions in which ALDEHYDES; KETONES; or reducing sugars react with the amino groups of AMINO ACIDS; PEPTIDES; PROTEINS; LIPIDS; or NUCLEIC ACIDS.The reaction with reducing sugars (glycation) results in formation of Schiff bases which undergo Amadori rearrangement and other reactions that result in the irreversible formation of ADVANCED GLYCATION END PRODUCTS (AGEs). Food browning, such as occurs when cooking with high heat (grilling, frying, roasting, etc.) is attributed to the Maillard reaction. Non-enzymatic glycation and subsequent formation of AGEs also occurs in vivo and is accelerated under hyperglycemic and inflammatory conditions, and OXIDATIVE STRESS.	Browning Reaction,Food Browning,Fructation,Glucation,Glycation,Lipid Glycation,Non-Enzymatic Glycation,Non-Enzymatic Glycosylation,Nonenzymatic Protein Glycation,Protein Glycation,Ribation,Browning Reactions,Browning, Food,Glycation, Lipid,Glycation, Non-Enzymatic,Glycation, Protein,Glycosylation, Non-Enzymatic,Non Enzymatic Glycation,Non Enzymatic Glycosylation,Protein Glycation, Nonenzymatic,Reaction, Browning,Reaction, Maillard,Reactions, Browning