Conservation of functional residues between yeast and E. coli inorganic pyrophosphatases.
The alignments of the amino acid sequences of inorganic pyrophosphatase (PPase) from Saccharomyces cerevisiae (Y1-PPase, 286 amino acids) and Escherichia coli (E-PPase, 175 amino acids) are examined in the light of crystallographic and chemical modification results placing specific amino acid residues at the active site of the yeast enzyme. The major results are: (1) the full E-PPase sequence aligns within residues 28-225 of Y1-PPase, raising the possibility that the N-terminal and C-terminal portions of Y1-PPase may not be essential for activity, and (2) that whereas the overall identity between the two sequences is only modest (22-27% depending on the choice of alignment parameters), of some 17 putative active site residues, 14-16 are identical between Y-PPase and E-PPase. PPase thus appears to be an example of enzymes from widely divergent species that conserve common functional elements within the context of substantial overall sequence variation.
Lahti
R
R
Department of Biochemistry, University of Turku, Finland.
Kolakowski
L F
LF
Heinonen
J
J
Vihinen
M
M
Pohjanoksa
K
K
Cooperman
B S
BS
D000595:Amino Acid Sequence; D001665:Binding Sites; D005075:Biological Evolution; D004926:Escherichia coli / Q000201:enzymology*; D043564:Inorganic Pyrophosphatase; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011755:Pyrophosphatases / Q000032:analysis / Q000235:genetics; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics; D013329:Structure-Activity Relationship; D013696:Temperature
D011755:Pyrophosphatases; D043564:Inorganic Pyrophosphatase