Disease relevance of Rhizomucor

• It has been applied to studies of the operational stability of lipases from Chromobacterium viscosum (lyophilized powder or polypropylene-adsorbed) and Rhizomucor miehei (Lipozyme) in different experimental conditions [1].
• A Rhizomucor miehei cDNA library constructed in Escherichia coli was screened with synthetic oligonucleotides designed from knowledge of a partial amino acid sequence of the secreted triglyceride lipase (triacylglycerol acylhydrolase EC 3.1.1.3) from this fungus [2].
• Cure of pulmonary Rhizomucor pusillus infection in a patient with hairy-cell leukemia: role of liposomal amphotericin B and GM-CSF [3].
• Absidia cylindrospora and Rhizomucor pusillus causal agents of phycomycoses, were cultured on sterile natural keratins in a mineral solution and the keratin degradation products analyzed [4].

Psychiatry related information on Rhizomucor

• Lipase catalyzed acidolysis of triacylglycerols (TAG) of soybean oil with oleic acid in organic solvent was studied; immobilized lipase from Rhizomucor miehei was used and the effects of reaction time, incubation temperature and enzyme load on TAG total and positional fatty acid (FA) percentage compositions were investigated [5].

High impact information on Rhizomucor

• X-ray analysis has revealed the atomic structures of two triacylglycerol lipases, unrelated in sequence: the human pancreatic lipase (hPL)4, and an enzyme isolated from the fungus Rhizomucor (formerly Mucor) miehei (RmL) [6].
• In the present study, the stereoselectivity of Rhizomucor miehei lipase, lipoprotein lipase, Candida antarctica B lipase, and human gastric lipase towards racemic dicaprin spread as a monolayer at the air-water interface was investigated [7].
• Crystal structure of the aspartic proteinase from Rhizomucor miehei at 2.15 A resolution [8].
• The crystal structure of the aspartic proteinase from Rhizomucor miehei (RMP, EC 3. 4. 23. 23) has been refined to 2.15 A resolution to a crystallographic R-value of 0.215 and an Rfree of 0.281 [8].
• The disulfide structure of sillucin, a highly knotted, cysteine-rich, antimicrobial peptide, isolated from Rhizomucor pusillus, has been determined to be Cys2--Cys7, Cys12--Cys24, Cys13--Cys30, and Cys14--Cys21 by disulfide mass mapping based on partial reduction and CN-induced cleavage enabled by cyanylation [9].

Biological context of Rhizomucor

• The genomic DNA and cDNA encoding an ALG2 homologue were cloned from the zygomycete fungus, Rhizomucor pusillus, and their nucleotide sequences were determined [10].
• To assess if the glyceryl esters could present a higher stability towards hydrolysis by lipases in the stratum corneum, hydrolysis rates were determined in vitro using a commercial fungal lipase from Rhizomucor miehei [11].
• Genetic transformation of a Rhizomucor pusillus mutant defective in asparagine-linked glycosylation: production of a milk-clotting enzyme in a less-glycosylated form [12].
• Substrate specificity of the alpha-L-arabinofuranosidase from Rhizomucor pusillus HHT-1 [13].
• Lipases from Rhizomucor miehei (Lipozyme IM20) and porcine pancreas (PPL) were employed as catalysts for the esterification reaction between the hydroxyl group of lactic acid and the carboxyl group of organic acids [14].

Anatomical context of Rhizomucor

• Preparation of stearoyl lactic acid ester catalyzed by lipases from Rhizomucor miehei and porcine pancreas optimization using response surface methodology [15].

Associations of Rhizomucor with chemical compounds

• We report on molecular dynamics simulations of a medium-sized protein, a lipase from Rhizomucor miehei, in vacuum, in water, and in a nonpolar solvent, methyl hexanoate [16].
• The crystal structure of an extracellular triglyceride lipase (from a fungus Rhizomucor miehei) inhibited irreversibly by diethyl p-nitrophenyl phosphate (E600) was solved by X-ray crystallographic methods and refined to a resolution of 2.65 A [17].
• The zygomycete fungus Rhizomucor pusillus secretes an aspartic proteinase (MPP) that contains asparagine ( N )-linked oligosaccharides at two sites [18].
• Differentiation of Rhizomucor species on the basis of their different sensitivities to lovastatin [19].
• METHODS: Four Rhizomucor spp. isolates were included to study the suitability of the three susceptibility testing methods to detect isolates resistant to voriconazole [20].

Gene context of Rhizomucor

• An intriguing result was the detection of a viral peptide of 53 amino acid residues (ORF 160L) showing high homology (identity/similarity: 60.0%/30.0%) to sillucin, an antibiotic peptide encoded by Rhizomucor pusillus [21].
• Crystals of Rhizomucor miehei aspartic proteinase (RMP) complexed with pepstatin A grew in the orthorhombic space group P212121 and were isomorphous to native RMP crystals [22].
• These observations suggest that the processing of mannose residues in asparagine-linked oligosaccharides in the Golgi apparatus of Rhizomucor resembles that in mammalian cells [23].
• A series of 1,3-diacylglycero-2-phosphocholines (1,3-PCs) with acyl chain lengths of C8-C18 were synthesised by chemical introduction of the phosphocholine moiety into the regioisomerically pure 1,3-diacylglycerols, which were obtained from glycerol and the vinyl esters of fatty acid by means of lipase from Rhizomucor mihei [24].
• Cloning and sequence analysis of the glyceraldehyde-3-phosphate dehydrogenase gene from the zygomycetes fungus Rhizomucor miehei [25].

Analytical, diagnostic and therapeutic context of Rhizomucor

• Site-directed mutagenesis was carried out to investigate the functional role of this residue in Rhizomucor pusillus pepsin, an aspartic proteinase with high milk-clotting activity produced by the fungus Rhizomucor pusillus [26].

References