Fructose-1,6-bisphosphatase. Primary structure of the rabbit liver enzyme. 'Intermediate' variability of an oligomeric protein.
The primary structure of rabbit liver fructose-1,6-bisphosphatase was determined by peptide analysis of digests with different proteases. The results establish the primary structure, complete data bank entries, and show that this enzyme variant is indeed homologous with other liver fructose-1,6-bisphosphatases. Residue differences with the enzymes from other mammals are 9-15%, with those from plants and yeasts about 50%, and with those from characterized prokaryotes up to 70%, showing an enzyme variability intermediate between those of 'variable' and 'constant' oligomeric dehydrogenases. Structural relationships, conformations and catalytic mechanisms are consistent within the family of fructose-1,6-bisphosphatases, and the rabbit protein is a typical rather than an aberrant form of the enzyme.
Kaiser
R
R
Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, Sweden.
Olsson
H
H
Erman
M
M
Weeks
C M
CM
Hjelmqvist
L
L
Ghosh
D
D
Jörnvall
H
H
D000249:Adenosine Monophosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002851:Chromatography, High Pressure Liquid; D010450:Endopeptidases / Q000378:metabolism; D006597:Fructose-Bisphosphatase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D008099:Liver / Q000201:enzymology*; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry; D011817:Rabbits; D017386:Sequence Homology, Amino Acid
D010455:Peptides; D000249:Adenosine Monophosphate; D006597:Fructose-Bisphosphatase; D010450:Endopeptidases