The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
MeSH Review


Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Rhizomucor


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


Anatomical context of Rhizomucor


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


  1. Development of small-size tubular-flow continuous reactors for the analysis of operational stability of enzymes in low-water systems. Pirozzi, D., Halling, P.J. Biotechnol. Bioeng. (2001) [Pubmed]
  2. Rhizomucor miehei triglyceride lipase is synthesized as a precursor. Boel, E., Huge-Jensen, B., Christensen, M., Thim, L., Fiil, N.P. Lipids (1988) [Pubmed]
  3. Cure of pulmonary Rhizomucor pusillus infection in a patient with hairy-cell leukemia: role of liposomal amphotericin B and GM-CSF. Ma, B., Seymour, J.F., Januszewicz, H., Slavin, M.A. Leuk. Lymphoma (2001) [Pubmed]
  4. Keratinolysis by Absidia cylindrospora and Rhizomucor pusillus: biochemical proof. Rajak, R.C., Malviya, H.K., Deshpande, H., Hasija, S.K. Mycopathologia (1992) [Pubmed]
  5. Biocatalyzed acidolysis of soybean oil triacylglycerols to increase oleic acid content. Cossignani, L., Damiani, P., Simonetti, M.S., Manes, J. Journal of chromatography. A. (2004) [Pubmed]
  6. A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex. Brzozowski, A.M., Derewenda, U., Derewenda, Z.S., Dodson, G.G., Lawson, D.M., Turkenburg, J.P., Bjorkling, F., Huge-Jensen, B., Patkar, S.A., Thim, L. Nature (1991) [Pubmed]
  7. Controlling lipase stereoselectivity via the surface pressure. Rogalska, E., Ransac, S., Verger, R. J. Biol. Chem. (1993) [Pubmed]
  8. Crystal structure of the aspartic proteinase from Rhizomucor miehei at 2.15 A resolution. Yang, J., Teplyakov, A., Quail, J.W. J. Mol. Biol. (1997) [Pubmed]
  9. Determination of the disulfide structure of sillucin, a highly knotted, cysteine-rich peptide, by cyanylation/cleavage mass mapping. Qi, J., Wu, J., Somkuti, G.A., Watson, J.T. Biochemistry (2001) [Pubmed]
  10. Characterization of alg2 encoding a mannosyltransferase in the zygomycete fungus Rhizomucor pusillus. Yamazaki, H., Shiraishi, N., Takeuchi, K., Ohnishi, Y., Horinouchi, S. Gene (1998) [Pubmed]
  11. A new sunscreen of the cinnamate class: synthesis and enzymatic hydrolysis evaluation of glyceryl esters of p-methoxycinnamic acid. de Freitas, Z.M., dos Santos, E.P., da Rocha, J.F., Dellamora-Ortiz, G.M., Gonçalves, J.C. European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences. (2005) [Pubmed]
  12. Genetic transformation of a Rhizomucor pusillus mutant defective in asparagine-linked glycosylation: production of a milk-clotting enzyme in a less-glycosylated form. Yamazaki, H., Ohnishi, Y., Takeuchi, K., Mori, N., Shiraishi, N., Sakata, Y., Suzuki, H., Horinouchi, S. Appl. Microbiol. Biotechnol. (1999) [Pubmed]
  13. Substrate specificity of the alpha-L-arabinofuranosidase from Rhizomucor pusillus HHT-1. Rahman, A.K., Kato, K., Kawai, S., Takamizawa, K. Carbohydr. Res. (2003) [Pubmed]
  14. Lipase catalyzed synthesis of organic acid esters of lactic acid in non-aqueous media. Kiran, K.R., Divakar, S. J. Biotechnol. (2001) [Pubmed]
  15. Preparation of stearoyl lactic acid ester catalyzed by lipases from Rhizomucor miehei and porcine pancreas optimization using response surface methodology. Kiran, K.R., Karanth, N.G., Divakar, S. Appl. Microbiol. Biotechnol. (1999) [Pubmed]
  16. Molecular dynamics simulations of an enzyme surrounded by vacuum, water, or a hydrophobic solvent. Norin, M., Haeffner, F., Hult, K., Edholm, O. Biophys. J. (1994) [Pubmed]
  17. Catalysis at the interface: the anatomy of a conformational change in a triglyceride lipase. Derewenda, U., Brzozowski, A.M., Lawson, D.M., Derewenda, Z.S. Biochemistry (1992) [Pubmed]
  18. Characterization of an alg2 mutant of the zygomycete fungus Rhizomucor pusillus. Takeuchi, K., Yamazaki, H., Shiraishi, N., Ohnishi, Y., Nishikawa, Y., Horinouchi, S. Glycobiology (1999) [Pubmed]
  19. Differentiation of Rhizomucor species on the basis of their different sensitivities to lovastatin. Lukács, G., Papp, T., Nyilasi, I., Nagy, E., Vágvölgyi, C. J. Clin. Microbiol. (2004) [Pubmed]
  20. A comparative study of the disc diffusion method with the broth microdilution and Etest methods for voriconazole susceptibility testing of Aspergillus spp. Serrano, M.C., Ramírez, M., Morilla, D., Valverde, A., Chávez, M., Espinel-Ingroff, A., Claro, R., Fernández, A., Almeida, C., Martín-Mazuelos, E. J. Antimicrob. Chemother. (2004) [Pubmed]
  21. Analysis of the first complete DNA sequence of an invertebrate iridovirus: coding strategy of the genome of Chilo iridescent virus. Jakob, N.J., Müller, K., Bahr, U., Darai, G. Virology (2001) [Pubmed]
  22. Structure of the Rhizomucor miehei aspartic proteinase complexed with the inhibitor pepstatin A at 2.7 A resolution. Yang, J., Quail, J.W. Acta Crystallogr. D Biol. Crystallogr. (1999) [Pubmed]
  23. Structure of asparagine-linked oligosaccharides of an aspartic proteinase from the zygomycete fungus Rhizomucor pusillus. Murakami, K., Takeuchi, K., Beppu, T., Horinouchi, S. Microbiology (Reading, Engl.) (1998) [Pubmed]
  24. 1,3-Diacylglycero-2-phosphocholines--synthesis, aggregation behaviour and properties as inhibitors of phospholipase D. Haftendorn, R., Schwarze, G., Ulbrich-Hofmann, R. Chem. Phys. Lipids (2000) [Pubmed]
  25. Cloning and sequence analysis of the glyceraldehyde-3-phosphate dehydrogenase gene from the zygomycetes fungus Rhizomucor miehei. Vastag, M., Kasza, Z., Acs, K., Papp, T., Schwab, H., Vágvölgyi, C. Antonie Van Leeuwenhoek (2004) [Pubmed]
  26. Involvement of a residue at position 75 in the catalytic mechanism of a fungal aspartic proteinase, Rhizomucor pusillus pepsin. Replacement of tyrosine 75 on the flap by asparagine enhances catalytic efficiency. Park, Y.N., Aikawa, J., Nishiyama, M., Horinouchi, S., Beppu, T. Protein Eng. (1996) [Pubmed]
WikiGenes - Universities