Fructose‐1,6‐bisphosphatase. Primary structure of the rabbit liver enzyme. ‘Intermediate’ variability of an oligomeric protein

Abstract

The primary structure of rabbit liver fructose-l,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-l,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-l,6-bisphosphatases, and the rabbit protein is a typical rather than an aberrant form of the enzyme.

Expression of fructose 1,6-bisphosphatase and phosphofructokinase is induced in hepatopancreas of the white shrimp Litopenaeus vannamei by hypoxia

“…The irreversible steps in glycolysis are by-passed in gluconeogenesis by pyruvate carboxylase (PC), phosphoenolpyruvate carboxykinase (PEPCK), fructose 1, 6-bisphosphatase (FBP) and glucose 6-phosphatase (GP). FBP is recognized as a key enzyme for gluconeogenesis (Lozinska-Gabska et al, 2003;Kaiser et al, 1996) and catalyzes the production of fructose 6-phosphate from fructose 1,6-bisphosphate. FBP appears to be present in all living organisms with the exception of archaebacteria whose FBP activity resides on a non-homologous protein (Stec et al, 2000).…”

Alcoholytic deblocking of N‐terminally acetylated peptides and proteins for sequence analysis

“…The preparation containing b)th isozymes was analyzed for 13 cycles revealing isozyme r, sidue differences at positions 1, 3 and 13 (Table 1). An /~-terminally acetylated fructose-l,6-bisphosphatase purified f~om rabbit liver [10] was also tested. After treatment of the e lzyme with TFA/methanol, Edman degradation revealed the s~quence Ala-Asp-Lys-which shows that the method also orks for acetylated N-terminal residues other than Ser and q hr.…”

“…The polypeptides employed were obtained from natural sources [6][7][8][9][10][11] or prepared synthetically [15]. Samples for deacetylation were either recovered in solution from column separations and lyophilized in glass tubes, directly spotted onto sequencer filters, or electroblotted to sequencer filters after SDS-polyacrylamide gel separation [16].…”

Molecular Cloning, Expression and Purification of Muscle Fructose-1,6-Bisphosphatase from Zaocys dhumnades: the Role of the N-Terminal Sequence in AMP Activation at Alkaline pH

“…The complete amino acid sequences of Fru-1,6-P 2 ase from several animal tissues such as porcine kidney (Marcus et al, 1982), sheep liver (Fisher and Thompson, 1983), rat liver , rabbit liver (Kaiser et al, 1996), human liver (El-Maghrabi et al, 1993), human muscle (Tillmann and Eschrich, 1998) and human lung (Skalecki et al, 1999) have been determined, and share approximately 80% homology, along with almost complete identity of the residues around both the active and allosteric sites. The sequences of the enzyme from plants including wheat (Raines et al, 1988), spinach (Marcus and Harrsch, 1990), potato (Koßmann et al, 1992), rapeseed (Rodriguez-Suarez and Wolosiuk, 1993) and pea (Carrasco et al, 1994), as well as yeast (Rogers et al, 1988) and E. coli (Hamilton et al, 1988), have approximately the same degree of homology.…”