Biomaterial Database

Isolation of mutations in Dictyostelium discoideum affecting alpha-mannosidase. 1974

S J Free, and W F Loomis

UI	MeSH Term	Description	Entries
D007527	Isoenzymes	Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.	Alloenzyme,Allozyme,Isoenzyme,Isozyme,Isozymes,Alloenzymes,Allozymes
D008361	Mannosidases	Glycoside hydrolases that catalyze the hydrolysis of alpha or beta linked MANNOSE.	Mannosidase
D009154	Mutation	Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.	Mutations
D009235	Myxomycetes	A division of organisms that exist vegetatively as complex mobile plasmodia, reproduce by means of spores, and have complex life cycles. They are now classed as protozoa but formerly were considered fungi.	Myxomycota,Protosteliomycetes,Slime Molds, Plasmodial,Slime Molds, True,Mold, Plasmodial Slime,Mold, True Slime,Molds, Plasmodial Slime,Molds, True Slime,Myxomycete,Myxomycotas,Plasmodial Slime Mold,Plasmodial Slime Molds,Protosteliomycete,Slime Mold, Plasmodial,Slime Mold, True,True Slime Mold,True Slime Molds
D004023	Dictyostelium	A genus of protozoa, formerly also considered a fungus. Its natural habitat is decaying forest leaves, where it feeds on bacteria. D. discoideum is the best-known species and is widely used in biomedical research.	Dictyostelium discoideum,Dictyostelium discoideums,Dictyosteliums,discoideum, Dictyostelium
D005959	Glucosidases	Enzymes that hydrolyze O-glucosyl-compounds. (Enzyme Nomenclature, 1992) EC 3.2.1.-.	Glucosidase
D006863	Hydrogen-Ion Concentration	The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH	pH,Concentration, Hydrogen-Ion,Concentrations, Hydrogen-Ion,Hydrogen Ion Concentration,Hydrogen-Ion Concentrations
D000118	Acetylglucosaminidase	A beta-N-Acetylhexosaminidase that catalyzes the hydrolysis of terminal, non-reducing 2-acetamido-2-deoxy-beta-glucose residues in chitobiose and higher analogs as well as in glycoproteins. Has been used widely in structural studies on bacterial cell walls and in the study of diseases such as MUCOLIPIDOSIS and various inflammatory disorders of muscle and connective tissue.	N-Acetyl-beta-D-glucosaminidase,Chitobiase,N,N-Diacetylchitobiase,N-Ac-beta-Glucosaminidase,NAGase,beta-D-Acetamido-2-Deoxyglucosidase,beta-D-N-acetylglucosaminidase,beta-N-Acetylglucosaminidase,N Ac beta Glucosaminidase,N Acetyl beta D glucosaminidase,N,N Diacetylchitobiase,beta D Acetamido 2 Deoxyglucosidase,beta D N acetylglucosaminidase,beta N Acetylglucosaminidase
D000469	Alkaline Phosphatase	An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.1.
D013913	Threonine Dehydratase	A pyridoxal-phosphate protein that catalyzes the deamination of THREONINE to 2-ketobutyrate and AMMONIA. The role of this enzyme can be biosynthetic or biodegradative. In the former role it supplies 2-ketobutyrate required for ISOLEUCINE biosynthesis, while in the latter it is only involved in the breakdown of threonine to supply energy. This enzyme was formerly listed as EC 4.2.1.16.	Threonine Deaminase,Threonine Dehydrase,Threonine Ammonia-Lyase,Ammonia-Lyase, Threonine,Deaminase, Threonine,Dehydrase, Threonine,Dehydratase, Threonine,Threonine Ammonia Lyase