Exo-(1-4)-α-D-glucan lyase
| Exo-(1→4)-α-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 | ||||||||
| |||||||||
The enzyme exo-(1→4)-α-D-glucan lyase (EC 4.2.2.13, α-(1→4)-glucan 1,5-anhydro-D-fructose eliminase, α-1,4-glucan exo-lyase, α-1,4-glucan lyase, GLase) is an enzyme with systematic name (1→4)-α-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 α-glucan = (n-1) 1,5-anhydro-D-fructose + D-glucose
The enzyme catalyses the sequential degradation of (1→4)-α-D-glucans from the non-reducing end.
References[edit]
- ^ Yu S, Kenne L, Pedersén M (March 1993). "Alpha-1,4-glucan lyase, a new class of starch/glycogen degrading enzyme. I. Efficient purification and characterization from red seaweeds". Biochimica et Biophysica Acta (BBA) - General Subjects. 1156 (3): 313–20. doi:10.1016/0304-4165(93)90049-e. PMID 8461323.
- ^ Yu S, Pedersén M (1993). "Alpha-1,4-glucan lyase, a new class of starch/glycogen-degrading enzyme. II. Subcellular localization and partial amino-acid sequence". Planta. 191 (1): 137–42. doi:10.1007/bf00240905. PMID 7763826. S2CID 39773299.
- ^ Yu S, Ahmad T, Kenne L, Pedersén M (May 1995). "alpha-1,4-Glucan lyase, a new class of starch/glycogen degrading enzyme. III. Substrate specificity, mode of action, and cleavage mechanism". Biochimica et Biophysica Acta (BBA) - General Subjects. 1244 (1): 1–9. doi:10.1016/0304-4165(94)00202-9. PMID 7766642.
- ^ Yu S, Christensen TM, Kragh KM, Bojsen K, Marcussen J (May 1997). "Efficient purification, characterization and partial amino acid sequencing of two alpha-1,4-glucan lyases from fungi". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1339 (2): 311–20. doi:10.1016/s0167-4838(97)00014-9. PMID 9187252.
- ^ Yu S, Bojsen K, Svensson B, Marcussen J (August 1999). "alpha-1,4-glucan lyases producing 1,5-anhydro-D-fructose from starch and glycogen have sequence similarity to alpha-glucosidases". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1433 (1–2): 1–15. doi:10.1016/s0167-4838(99)00152-1. PMID 10446355.
- ^ Lee SS, Yu S, Withers SG (May 2002). "alpha-1,4-Glucan lyase performs a trans-elimination via a nucleophilic displacement followed by a syn-elimination". Journal of the American Chemical Society. 124 (18): 4948–9. doi:10.1021/ja0255610. PMID 11982345.
- ^ Lee SS, Yu S, Withers SG (November 2003). "Detailed dissection of a new mechanism for glycoside cleavage: alpha-1,4-glucan lyase". Biochemistry. 42 (44): 13081–90. doi:10.1021/bi035189g. PMID 14596624.
External links[edit]
- Exo-(1->4)-alpha-D-glucan+lyase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
