Disease relevance of Neocallimastix

• Clostridium beijerinckii cells expressing Neocallimastix patriciarum glycoside hydrolases show enhanced lichenan utilization and solvent production [1].
• Cloning and expression of multiple cellulase cDNAs from the anaerobic rumen fungus Neocallimastix patriciarum in Escherichia coli [2].

High impact information on Neocallimastix

• Characteristic inhibitors of mitochondrial AACs blocked adenine nucleotide exchange by the Neocallimastix protein [3].
• A mitochondrial-like targeting signal on the hydrogenosomal malic enzyme from the anaerobic fungus Neocallimastix frontalis: support for the hypothesis that hydrogenosomes are modified mitochondria [4].
• Intronless celB from the anaerobic fungus Neocallimastix patriciarum encodes a modular family A endoglucanase [5].
• Glucose metabolic pathways in the anaerobic rumen fungus Neocallimastix frontalis EB188 [6].
• The presence of a [Fe]-hydrogenase in the hydrogenosomes of the anaerobic chytridiomycete fungus Neocallimastix sp. L2 has been demonstrated by immunocytochemistry, subcellular fractionation, Western-blotting and measurements of hydrogenase activity in the presence of various concentrations of carbon monoxide (CO) [7].

Biological context of Neocallimastix

• The cDNA designated celB from the anaerobic rumen fungus Neocallimastix patriciarum contained a single open reading frame of 1422 bp coding for a protein (CelB) of M(r) 53,070 [5].
• The nucleotide sequence of the cDNA of the phosphoenolpyruvate carboxykinase-encoding gene from the fungus Neocallimastix frontalis, was determined [8].
• Sequence of the phosphoenolpyruvate carboxykinase-encoding cDNA from the rumen anaerobic fungus Neocallimastix frontalis: comparison of the amino acid sequence with animals and yeast [8].
• A DNA clone containing a putative enolase gene was isolated from a genomic DNA library of the anaerobic fungus Neocallimastix frontalis [9].
• A clone containing a Neocallimastix frontalis cDNA assumed to encode the beta subunit of succinyl-CoA synthetase (SCSB) was identified by sequence homology with prokaryotic and eukaryotic counter-parts [10].

Associations of Neocallimastix with chemical compounds

• Cellulases from the ruminal fungus Neocallimastix frontalis EB188 were separated by using hydroxylapatite column chromatography [11].
• Two extracellular feruloyl esterases (FAE-I and FAE-II) produced by the anaerobic fungus Neocallimastix strain MC-2 which cleave ferulic acid from O-(5-O-[(E)-feruloyl]-alpha-L- arabinofuranosyl)-(1-->3)-O-beta-D-xylopyranosyl-(1-->4)-D-xylopyranose (FAXX) were purified [12].
• Neocallimastix frontalis PN-1 utilized the soluble sugars D-glucose, D-cellobiose, D-fructose, maltose, sucrose, and D-xylose for growth [13].
• scsB, a cDNA encoding the hydrogenosomal beta subunit of succinyl-CoA synthetase from the anaerobic fungus Neocallimastix frontalis [10].
• The range of polysaccharide-degrading enzymes formed by three anaerobic rumen fungi (Neocallimastix patriciarum, Piromonas communis, and an unidentified isolate (F] was monitored following growth on seven mono-, di-, and poly-saccharide carbohydrate substrates [14].

Gene context of Neocallimastix

• The hydrogenosomal malic enzyme (ME) was purified from the anaerobic fungus Neocallimastix frontalis [4].
• Purification and partial characterization of two feruloyl esterases from the anaerobic fungus Neocallimastix strain MC-2 [12].
• The nucleotide sequence of a cellulase cDNA (celA) from the rumen fungus Neocallimastix patriciarum and the primary structure of the protein which it encodes were characterized [15].
• Neocallimastix frontalis enolase gene, enol: first report of an intron in an anaerobic fungus [9].
• The sequence of the Neocallimastix frontalis enolase gene promoter was determined up to 1800 nucleotides 5' to the major transcriptional start point [16].

Analytical, diagnostic and therapeutic context of Neocallimastix

• The genetic similarity of different generations of Neocallimastix frontalis SK was examined by random amplified polymorphic DNA (RAPD) profiling and internal transcribed spacer 1 (ITS1) sequence analysis [17].

References