Neurospora amino acid sequence

Lerch, K. (1982). Primary structure of tyrosinase from Neurospora crassa. II. Complete amino acid sequence and chemical structure of a tripeptide containing an unusual thioether. J. Biol. Chem., 257, 6414-6419. 

Fig. 10.3 Amino acid sequences of CuZn-SODs from various organisms.31 Yeast, Saccharomyces cerevisiae Neurospora, Neurospora crassa Arabido., Arabidopsis thaliana Cyt, cytosolic CuZn-SOD Chi, chloroplastic CuZn-SOD. Amino acid residue number is based on that of human CuZn-SOD. Residues conserved in all species are boxed.

The amino acid sequences of three GDH s have been determined these are presented in Figs. 4 and 5, with B representing the bovine (258), C the chicken (258), and N the Neurospora NADP-dependent enzyme (259). Some peptides obtained from the rat liver enzyme (R) are also shown (260) in this instance the tryptic peptides have been placed only by homology. 

The MW of the NADP-specific GDH of Neurospora has been shown to be 280,000-296,000 by sedimentation equilibrium analysis (Wootten, 1973) while the amino acid sequence (Wootten et al., 1974) shows that the polypeptides possess 50 residues less than those of the bovine liver enzyme, and that each subunit has a MW of 48,438 showing that this enzyme also is hexameric. The NADP-specific enzymes of Baker s yeast, E. coli, and the enzyme of dual coenzyme specificity from Mycoplasma laidlawii have been shown to have molecular weights similar to the Neurospora NADP enzyme, while SDS electrophoresis has shown their subunits are also of a similar size (Smith et al., 1975). 

Fig. 19. Alignment of homospermidine synthase (HSS) amino acid sequence from Senecio ver-nalis (Sv) in comparison to deoxyhypusine synthase amino acid sequences from six different species. Sv, Senecio vernalis Nt, Nicotiana tabacumi Hs, Homo sapiens Sc, Saccharomyces cerevisiae Nc, Neurospora crassa Mj, Methanococcus jannaschii. Black boxes denote identical amino acid residues in all seven sequences, framed boxes conservative replacement...

The active site of Neurospora PPO is thought to contain two mols copper/mol active site (Solomon, 1981) Elucidation of the complete amino acid sequence of Neurospora PPO (Lerch, 1978), coupled with dye-sensitized photooxidation (Pfiffner and Lerch, 1981) and inhibition (Pfiffner et al , 1981) indicated that... 

Lerch, K., 1978, Amino acid sequence of tyrosinase from Neurospora crassa, Proc. Natl. Acad. Sci. USA 75 3635. 

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. 

Fig. 1 Blocks of multiple sequence alignment of protein sequences of carboxypeptidases from B. taurus, Mus musculus, Rattus norvegicus, Neurospora crassa, Schizosaccharomyces pombe, Drosophila melanogaster, and Homo sapiens along with protein sequence from H. pylori (Uniprot accession code HPAG1 0372 from strain HPAG1). Numbers on the top correspond to amino acid residue number of the carboxypeptidase enzyme from B. taurus. Gray vertical columns indicate conserved residues. Amino acid residues corresponding to Glu-182 and His-306, which coordinate to zinc, are conserved, whereas another Zn-coordinating amino acid residue corresponding to His-179 is substituted by Gin in the Helicobacter sequence. Functionally important residues corresponding to Arg-237 are also conserved...

The chemical reactions for the conversion of homoserine to a-ketobutyric acid in the vertebrate organism, if that is the pathway, are quite obscure. In Neurospora homoserine is the precursor of threonine (see the chapter, Synthetic Processes Involving Amino Acids, which in turn is deaminated to a-ketobutyric acid (see Fig. 3, reaction 4). The reaction sequence from homoserine to threonine probably is through/3-y-dihydroxy-a-aminobutyric acid as an intermediate. 

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