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- *******************************************
- * Fructose-1-6-bisphosphatase active site *
- *******************************************
-
- Fructose-1,6-bisphosphatase (EC 3.1.3.11) (FBPase) [1], a regulatory enzyme in
- gluconeogenesis, catalyzes the hydrolysis of fructose 1,6-bisphosphate to
- fructose 6-phosphate. It is involved in many different metabolic pathways and
- found in most organisms.
-
- In mammalian FBPase, a lysine residue has been shown to be involved in the
- catalytic mechanism [2]. The region around this residue is highly conserved
- and can be used as a signature pattern for FBPase. It must be noted that, in
- some bacterial FBPase sequences, the active site lysine is replaced by an
- arginine.
-
- -Consensus pattern: G-[RK]-L-x(1,2)-[LIV]-Y-E-x(2)-P-[LIVM]-[SA]
- [K/R is the active site residue]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
- -Last update: June 1994 / Pattern and text revised.
-
- [ 1] Benkovic S.J., DeMaine M.M.
- Adv. Enzymol. 53:45-82(1982).
- [ 2] Ke H., Thorpe C.M., Seaton B.A., Lipscomb W.N., Marcus F.
- J. Mol. Biol. 212:513-539(1989).
- [ 3] Gibson J.L., Chen J.-H., Tower P.A., Tabita F.R.
- Biochemistry 29:8085-8093(1990).
-