Escherichia coli K-12 substr. MG1655 Reaction:

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number:

Enzymes and Genes:
maltodextrin phosphorylaseInferred from experiment: malP

In Pathway: glycogen degradation I

Note that this reaction equation differs from the official Enzyme Commission reaction equation for this EC number, which can be found here .

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

Mass balance status: Balanced.

Enzyme Commission Primary Name: glycogen phosphorylase

Enzyme Commission Synonyms: muscle phosphorylase a and b, amylophosphorylase, polyphosphorylase, amylopectin phosphorylase, glucan phosphorylase, α-glucan phosphorylase, 1,4-α-glucan phosphorylase, glucosan phosphorylase, granulose phosphorylase, maltodextrin phosphorylase, muscle phosphorylase, myophosphorylase, potato phosphorylase, starch phosphorylase, 1,4-α-D-glucan:phosphate α-D-glucosyltransferase, phosphorylase (ambiguous)

Enzyme Commission Summary:
This entry covers several enzymes from different sources that act in vivo on different forms of (1→4)-α-D-glucans. Some of these enzymes catalyse the first step in the degradation of large branched glycan polymers - the phosphorolytic cleavage of α-1,4-glucosidic bonds from the non-reducing ends of linear poly(1→4)-α-D-glucosyl chains within the polymers. The enzyme stops when it reaches the fourth residue away from an α-1,6 branching point, leaving a highly branched core known as a limit dextrin. The accepted name of the enzyme should be modified for each specific instance by substituting "glycogen" with the name of the natural substrate, e.g. maltodextrin phosphorylase, starch phosphorylase, etc.

Citations: [Baum53, Chen68a, Cowgill59, Fischer70, Green43, Hanes40]

Gene-Reaction Schematic

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:


Baum53: Baum H, Gilbert GA (1953). "A simple method for the preparation of crystalline potato phosphorylase and Q-enzyme." Nature 171(4361);983-4. PMID: 13063502

Chen68a: Chen GS, Segel IH (1968). "Purification and properties of glycogen phosphorylase from Escherichia coli." Arch Biochem Biophys 1968;127(1);175-86. PMID: 4878695

Cowgill59: Cowgill RW (1959). "Lobster muscle phosphorylase: purification and properties." J Biol Chem 234;3146-53. PMID: 13812491

Fischer70: Fischer EH, Pocker A, Saari JC (1970). "The structure, function and control of glycogen phosphorylase." In: Campbell, P.N. and Greville, G.D. (Eds), Essays in Biochemistry, vol. 6, Academic Press, London and New York, pp. 23-68.

Green43: Green AA, Cori GT (1943). "Crystalline muscle phosphorylase. I. Preparation, properties, and molecular weight." J. Biol. Chem. 151 21-29.

Hanes40: Hanes CS (1940). "The breakdown and synthesis of starch by an enzyme from pea seeds." Proc. R. Soc. Lond. B Biol. Sci. 128 421-450.

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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