Thermophilic bacillus AspAT

Recently, the primary structure of Thermophilic bacillus AspAT was deduced from its cDNA sequence.24 However, there was no significant sequence homology found between thermophilic enzyme and other AspAT s. After careful comparison among primary structures of AspAT s, we found that catalytically essential amino acid residues located at the active site in AspAT were also assigned in the thermophilic enzyme (Fig. 1.2). Although thermophilic AspAT is presumed to have an entirely different tertiary structure from other AspAT s, catalytically essential amino acid residues may be conserved in its structure. 

The primary structure of AspAT from Thermophilic bacillus was determined from cDNA sequence.24 Sequence information of an N-terminal portion of the native enzyme and 19 tryptic peptide fragments, recovered from HPLC, was obtained from gas phase sequencer analyses. Based on such sequence information, four oligonucleotide probes were prepared. cDNA encoding AspAT was cloned by screening restriction enzyme fragments from genomic cDNA of Thermophilic bacillus species YM-2. Amino acid sequence of Thermophilic bacillus AspAT deduced from cDNA was confirmed by the sequences made available by gas phase sequencer analysis. 

Abbreviations used cAspAT, pig cytosolic Asp AT mAspAT, pig mitochondrial AspAT eAspAT, co/i Asp AT eAroAT, cott AroAT t Asp AT, thermophilic Bacillus species. f2 Conserved amino acid residues found at the same residue number are marked , and those residues with high degree of replacement are shown in bold face. 

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See also in sourсe #XX -- [ , ]

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