Exo-(1-4)-α-D-glucan lyase

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 systematic 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

\rightleftharpoons

(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. doi:10.1016/0304-4165(93)90049-e. PMID 8461323.
↑ 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. doi:10.1007/bf00240905. PMID 7763826.
↑ Yu, S.; Ahmad, T.; Kenne, L.; 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. doi:10.1016/0304-4165(94)00202-9. PMID 7766642.
↑ Yu, S.; Christensen, T.M.; Kragh, K.M.; Bojsen, K.; 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. doi:10.1016/s0167-4838(97)00014-9. PMID 9187252.
↑ Yu, S.; Bojsen, K.; Svensson, B.; 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. doi:10.1016/s0167-4838(99)00152-1. PMID 10446355.
↑ Lee, S.S.; Yu, S.; 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. doi:10.1021/ja0255610. PMID 11982345.
↑ Lee, S.S.; Yu, S.; Withers, S.G. (2003). "Detailed dissection of a new mechanism for glycoside cleavage: α-1,4-glucan lyase". Biochemistry. 42: 13081–13090. doi:10.1021/bi035189g. PMID 14596624.

External links

[//www.nlm.nih.gov/cgi/mesh/2011/MB_cgi?mode=&term=Exo-(1->4)-alpha-D-glucan+lyase Exo-(1->4)-alpha-D-glucan lyase] at the US National Library of Medicine Medical Subject Headings (MeSH)

Carbon-oxygen lyases (EC 4.2) (primarily dehydratases)

4.2.1: Hydro-Lyases	Carbonic anhydrase Fumarase Aconitase Enolase Alpha Enolase 2 Enoyl-CoA hydratase/3-Hydroxyacyl ACP dehydrase Methylglutaconyl-CoA hydratase Tryptophan synthase Cystathionine beta synthase Porphobilinogen synthase 3-Isopropylmalate dehydratase Urocanase Uroporphyrinogen III synthase Nitrile hydratase

4.2.2: Acting on polysaccharides	Hyaluronate lyase

4.2.3: Acting on phosphates	Threonine synthase

4.2.99: Other	Carboxymethyloxysuccinate lyase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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