KEGG ENZYME: 4.2.2.13

ENZYME: 4.2.2.13

Entry

EC 4.2.2.13                 Enzyme

Name

exo-(1->4)-alpha-D-glucan lyase;
alpha-(1->4)-glucan 1,5-anhydro-D-fructose eliminase;
alpha-1,4-glucan exo-lyase;
alpha-1,4-glucan lyase;
GLase

Class

Lyases;
Carbon-oxygen lyases;
Acting on polysaccharides

Sysname

(1->4)-alpha-D-glucan exo-4-lyase (1,5-anhydro-D-fructose-forming)

Reaction(IUBMB)

linear alpha-glucan = (n-1) 1,5-anhydro-D-fructose + D-glucose

Substrate

linear alpha-glucan

Product

(n-1) 1,5-anhydro-D-fructose;
D-glucose [CPD:C00031]

Comment

The enzyme catalyses the sequential degradation of (1->4)-alpha-D-glucans from the non-reducing end with the release of 1,5-anhydro-D-fructose. Thus, for an alpha-glucan containing n (1->4)-linked glucose units, the final products are 1 glucose plus (n-1) 1,5-anhydro-D-fructose. Maltose, maltosaccharides and amylose are all completely degraded. It does not degrade (1->6)-alpha-glucosidic bonds and thus the degradation of a branched glucan, such as amylopectin or glycogen, will result in the formation of 1,5-anhydro-D-fructose plus a limit dextrin. Other enzymes involved in the anhydrofructose pathway are EC 4.2.1.110 (aldos-2-ulose dehydratase), EC 4.2.1.111 (1,5-anhydro-D-fructose dehydratase) and EC 5.3.2.7 (ascopyrone tautomerase).

History

EC 4.2.2.13 created 1999

Reference

1 [PMID:8461323]

Authors

Yu S, Kenne L, Pedersen M.

Title

Alpha-1,4-glucan lyase, a new class of starch/glycogen degrading enzyme. I. Efficient purification and characterization from red seaweeds.

Journal

Biochim Biophys Acta 1156:313-20 (1993)
DOI:10.1016/0304-4165(93)90049-E

Reference

2 [PMID:7763826]

Authors

Yu S, Pedersen M.

Title

Alpha-1,4-glucan lyase, a new class of starch/glycogen-degrading enzyme. II. Subcellular localization and partial amino-acid sequence.

Journal

Planta 191:137-42 (1993)
DOI:10.1007/bf00240905

Reference

3 [PMID:7766642]

Authors

Yu S, Ahmad T, Kenne L, Pedersen M.

Title

alpha-1,4-Glucan lyase, a new class of starch/glycogen degrading enzyme. III. Substrate specificity, mode of action, and cleavage mechanism.

Journal

Biochim Biophys Acta 1244:1-9 (1995)
DOI:10.1016/0304-4165(94)00202-9

Reference

4 [PMID:9187252]

Authors

Yu S, Christensen TM, Kragh KM, Bojsen K, Marcussen J.

Title

Efficient purification, characterization and partial amino acid sequencing of two alpha-1,4-glucan lyases from fungi.

Journal

Biochim Biophys Acta 1339:311-20 (1997)
DOI:10.1016/S0167-4838(97)00014-9

Reference

5 [PMID:10446355]

Authors

Yu S, Bojsen K, Svensson B, Marcussen J.

Title

alpha-1,4-glucan lyases producing 1,5-anhydro-D-fructose from starch and glycogen have sequence similarity to alpha-glucosidases.

Journal

Biochim Biophys Acta 1433:1-15 (1999)
DOI:10.1016/S0167-4838(99)00152-1

Reference

6 [PMID:11982345]

Authors

Lee SS, Yu S, Withers SG.

Title

alpha-1,4-Glucan lyase performs a trans-elimination via a nucleophilic displacement followed by a syn-elimination.

Journal

J Am Chem Soc 124:4948-9 (2002)
DOI:10.1021/ja0255610

Reference

7 [PMID:14596624]

Authors

Lee SS, Yu S, Withers SG.

Title

Detailed dissection of a new mechanism for glycoside cleavage: alpha-1,4-glucan lyase.

Journal

Biochemistry 42:13081-90 (2003)
DOI:10.1021/bi035189g

Other DBs

ExplorEnz - The Enzyme Database:

4.2.2.13

IUBMB Enzyme Nomenclature:

4.2.2.13

ExPASy - ENZYME nomenclature database:

4.2.2.13

UM-BBD (Biocatalysis/Biodegradation Database):

4.2.2.13

BRENDA, the Enzyme Database:

4.2.2.13

CAS:	148710-18-3

All links

Protein sequence (20)   
   PDBSTR (20)   
DNA sequence (16)   
   GenBank (8)   
   EMBL (8)   
3D Structure (5)   
   PDB (5)   
Enzyme (1)   
   UMBBD-EC (1)   
All databases (42)   

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