Candida amino acid sequence

We are interested in fatw acid oxidation by wild-type and mutant strains of the yeast Candida cloacae under industrial conditions. The aim is to efficiently generate novel compounds of fatty acid o ddation. To develop procedures for assaying an industrial fermentation, we have grown cultures of parent and mutant organisms under laboratoiy conditions and compared induction patterns o er time of several enzymes of fatty acid oxidation. We ha e purified alcohol oxidase, an enzyme in the m-oxidation pathway. The protein is of Mr 70 000 and oxidises long-chain fatty alcohols. Antibodies and amino acid sequence are being obtained to allow us to isolate the gene for this enzyme. 

The data presented in Table 3, which includes the amino acid composition of baker s yeast and Candida krusei cytochrome c for comparison, show that Ustilago and Neurospora cytochrome c contain the same number of total residues. In seven instances, the number of residues of a particular amino acid/mole are identical. Thus, even in the absence of a sequence for the Ustilago cytochrome it can be concluded that this protein, unlike the siderochromes, has suffered little alteration in the progression from the Ascomycetes to the Basidiomycetes. This can be ascribed to the varying function of the two types of molecules. Cytochrome c must fit into a relatively specific slot bounded by a reductase and an oxidase and it has hence evolved much more slowly than the more freely acting transport agents where the specificity constraints are less demanding. 

---