Exo-(1-4)-α-D-glucan lyase: Difference between revisions
Content deleted Content added
←Created page with '{{Infobox enzyme | Name = Exo-(1->4)-alpha-D-glucan lyase | EC_number = 4.2.2.13 | CAS_number = 148710-18-3 | IUBMB_EC_number = 4/2/2/13 | GO_code = | image = ...' |
(No difference)
|
Revision as of 22:57, 26 May 2013
| Exo-(1->4)-alpha-D-glucan lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.2.2.13 | ||||||||
| CAS no. | 148710-18-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Exo-(1->4)-alpha-D-glucan lyase (EC 4.2.2.13, alpha-(1->4)-glucan 1,5-anhydro-D-fructose eliminase, alpha-1,4-glucan exo-lyase, alpha-1,4-glucan lyase, GLase) is an enzyme with system name (1->4)-alpha-D-glucan exo-4-lyase (1,5-anhydro-D-fructose-forming).[1][2][3][4][5][6][7] This enzyme catalyses the following chemical reaction
- linear alpha-glucan (n-1) 1,5-anhydro-D-fructose + D-glucose
The enzyme catalyses the sequential degradation of (1->4)-alpha-D-glucans from the non-reducing end.
References
- ^ Yu, S., Kenne, L., Pedersén, M. (1993). "α-1,4-Glucan lyase, a new class of starch/glycogen degrading enzyme. I. Efficient purification and characterization from red seaweeds". Biochim. Biophys. Acta. 1156: 313–320. PMID 8461323.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Yu, S., Pedersén, M. (1993). "α-1,4-Glucan lyase, a new class of starch/glycogen degrading enzyme. II. Subcellular localization and partial amino-acid sequence". Planta. 191: 137–142. PMID 7763826.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Yu, S., Ahmad, T., Kenne, L. and Pedersén, M. (1995). "α-1,4-Glucan lyase, a new class of starch/glycogen degrading enzyme. III. Substrate specificity, mode of action, and cleavage mechanism". Biochim. Biophys. Acta. 1244: 1–9. PMID 7766642.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Yu, S., Christensen, T.M., Kragh, K.M., Bojsen, K. and Marcussen, J. (1997). "Efficient purification, characterization and partial amino acid sequencing of two α-1,4-glucan lyases from fungi". Biochim. Biophys. Acta. 1339: 311–320. PMID 9187252.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Yu, S., Bojsen, K., Svensson, B. and Marcussen, J. (1999). "α-1,4-glucan lyases producing 1,5-anhydro-D-fructose from starch and glycogen have sequence similarity to α-glucosidases". Biochim. Biophys. Acta. 1433: 1–15. PMID 10446355.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Lee, S.S., Yu, S. and Withers, S.G. (2002). "α-1,4-Glucan lyase performs a trans-elimination via a nucleophilic displacement followed by a syn-elimination". J. Am. Chem. Soc. 124: 4948–4949. PMID 11982345.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Lee, S.S., Yu, S. and Withers, S.G. (2003). "Detailed dissection of a new mechanism for glycoside cleavage: α-1,4-glucan lyase". Biochemistry. 42: 13081–13090. PMID 14596624.
{{cite journal}}: CS1 maint: multiple names: authors list (link)
External links
- Exo-(1->4)-alpha-D-glucan+lyase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)