Disease relevance of Geotrichum

• Tracing experiments were carried out to identify volatile and nonvolatile L-methionine degradation intermediates and end products in the yeast Geotrichum candidum and in the bacterium Brevibacterium linens, both of which are present in the surface flora of certain soft cheeses and contribute to the ripening reactions [1].

High impact information on Geotrichum

• Ser-His-Glu triad forms the catalytic site of the lipase from Geotrichum candidum [2].
• A novel oligoxyloglucan-specific glycosidase, oligoxyloglucan reducing end-specific cellobiohydrolase (OXG-RCBH), with a molecular mass of 97 kDa and a pI of 6.1, was isolated from the fungus Geotrichum sp. M128 [3].
• Does sequence similarity of human choline esterase, Torpedo acetylcholine esterase and Geotrichum candidum lipase reveal the active site serine residue [4]?
• Reduction of methyl ketones by dried cells of Geotrichum candidum (APG4) afforded (S)-alcohols in excellent enantiomeric excess (ee), whereas the reduction of trifluoromethyl ketones gave the corresponding alcohols of the opposite configuration also in excellent ee [5].
• JHE is a member of the alpha/beta hydrolase fold family of enzymes and was built according to two structures in the same family: acetylcholinesterase from Torpedo californica and lipase from Geotrichum candidum [6].

Biological context of Geotrichum

• The abilities of lipases produced by the fungus Geotrichum candidum to selectively fractionate mixtures of conjugated linoleic acid (CLA) isomers during esterification of mixed CLA free fatty acids and during hydrolysis of mixed CLA methyl esters were examined [7].
• The alkali-extracted water-soluble galactomannan F1SS isolated from the cell wall of two species each of Geotrichum, Galactomyces, and Dipodascus have been studied by methylation analysis and NMR spectroscopy, and their structure is established as the following: [carbohydrate structure: see text][8]
• The deduced amino acid sequence shares 99.5% overall identity with that of lipase II (GCL II) from Geotrichum candidum ATCC 34614, whereas TFL I is a trimer enzyme and GCL II monomer [9].

Associations of Geotrichum with chemical compounds

• Geotrichum candidum P-5 produces an intracellular serine protease resembling chymotrypsin [10].
• A total of 322 yeast strains and yeastlike organisms belonging to the genera Candida, Cryptococcus, Geotrichum, Saccharomyces, and Trichosporon were tested with the new monoclonal antibody-based Bichro-latex albicans and Krusei color latex tests [11].
• The affinity (KS value) of Geotrichum candidum for glucose determined from chemostate cultures was ca. 1 mg/1 [12].
• Diffusion of lactate and ammonium in relation to growth of Geotrichum candidum at the surface of solid media [13].
• All strains of Geotrichum candidum and many other yeast-like fungi assimilated acetoin and butan-2,3-diol [14].

Gene context of Geotrichum

• The updated Vitek Yeast Biochemical Card (YBC) was compared with the API 20C by using 409 germ tube-negative yeasts and Geotrichum spp. that were either clinical or proficiency sample isolates [15].
• Geotrichum silvicola sp. nov., a novel asexual arthroconidial yeast species related to the genus Galactomyces [16].
• The substrate profiles of Geotrichum candidum lipase obtained by both a titrimetric assay and the RTA assay indicated the highest activity against triolein [17].
• An extracellular lipase (EC 3.1.1.3) from Geotrichum marinum was purified 76-fold with 46% recovery using Octyl Sepharose 4 Fast Flow and Bio-Gel A 1.5 m chromatography [18].
• With guinea pig pancreatic lipase and with three mold lipases (Geotrichum candidum M, Geotrichum candidum A, and Candida antarctica B), the preference switches from sn-3 to sn-1 when the acyl chain length increases from eight to 18 carbon atoms [19].

Analytical, diagnostic and therapeutic context of Geotrichum

• Other members of the family that have been studied by X-ray crystallography include Torpedo californica acetylcholinesterase, Geotrichum candidum lipase and Candida rugosa lipase [20].

References