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- * Glycosyl hydrolases family 31 signatures *
- ********************************************
-
- It has been shown [1,2,3] that the following glycosyl hydrolases can be, on
- the basis of sequence similarities, classified into a single family:
-
- - Lysosomal alpha-glucosidase (EC 3.2.1.20) (acid maltase) is a vertebrate
- glycosidase active at low pH, which hydrolyzes alpha(1->4) and alpha(1->6)
- linkages in glycogen, maltose, and isomaltose.
- - Alpha-glucosidase (EC 3.2.1.20) from the yeast Candida tsukunbaensis.
- - Intestinal sucrase-isomaltase (EC 3.2.1.48 / EC 3.2.1.10) is a vertebrate
- membrane-bound, multifunctional enzyme complex which hydrolyzes sucrose,
- maltose and isomaltose. The sucrase and isomaltase domains of the enzyme
- are homologous (41% of amino acid identity) and have most probably evolved
- by duplication.
- - Glucoamylase 1 (EC 3.2.1.3) (glucan 1,4-alpha-glucosidase) from the yeast
- Schwanniomyces occidentalis.
-
- An aspartic acid has been implicated [4] in the catalytic activity of sucrase,
- isomaltase, and lysosomal alpha-glucosidase. The region around this active
- residue is highly conserved and can be used as a signature pattern. We have
- used a second region, which contains two conserved cysteines, as an additional
- signature pattern.
-
- -Consensus pattern: G-[LIVM]-W-x-D-M-N-E
- [D 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.
-
- -Consensus pattern: G-A-D-[LIVM]-C-G-F-x(3)-[ST]-x(3)-L-C-x-R-W-x(2)-L-G-[SA]-
- F-x-P-F-x-R-N
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -Expert(s) to contact by email: Henrissat B.
- bernie@cermav.grenet.fr
-
- -Last update: December 1992 / Patterns and text revised.
-
- [ 1] Henrissat B.
- Biochem. J. 280:309-316(1991).
- [ 2] Kinsella B.T., Hogan S., Larkin A., Cantwell B.A.
- Eur. J. Biochem. 202:657-664(1991).
- [ 3] Naim H.Y., Niermann T., kleinhans U., Hollenberg C.P.,
- Strasser A.W.M.
- FEBS Lett. 294:109-112(1991).
- [ 4] Hermans M.M.P., Kroos M.A., van Beeumen J., Oostra B.A., Reuser A.J.J.
- J. Biol. Chem. 266:13507-13512(1991).
-