From Wikipedia, the free encyclopedia
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
Search
PMC articles
PubMed articles
NCBI proteins

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

  1. ^ 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.
  2. ^ 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.
  3. ^ 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.
  4. ^ 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.
  5. ^ 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.
  6. ^ 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.
  7. ^ 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

From Wikipedia, the free encyclopedia
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
Search
PMC articles
PubMed articles
NCBI proteins

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

  1. ^ 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.
  2. ^ 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.
  3. ^ 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.
  4. ^ 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.
  5. ^ 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.
  6. ^ 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.
  7. ^ 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


Videos

Youtube | Vimeo | Bing

Websites

Google | Yahoo | Bing

Encyclopedia

Google | Yahoo | Bing

Facebook