Glucan phosphorylase [Carbohydrate transport and metabolism].

glycogen/starch/alpha-glucan phosphorylases. This family consists of phosphorylases. Members use phosphate to break alpha 1,4 linkages between pairs of glucose residues at the end of long glucose polymers, releasing alpha-D-glucose 1-phosphate. The nomenclature convention is to preface the name according to the natural substrate, as in glycogen phosphorylase, starch phosphorylase, maltodextrin phosphorylase, etc. Name differences among these substrates reflect differences in patterns of branching with alpha 1,6 linkages. Members include allosterically regulated and unregulated forms. A related family, TIGR02094, contains examples known to act well on particularly small alpha 1,4 glucans, as may be found after import from exogenous sources. [Energy metabolism, Biosynthesis and degradation of polysaccharides]

glycogen phosphorylase and similar proteins. This is a family of oligosaccharide phosphorylases. It includes yeast and mammalian glycogen phosphorylases, plant starch/glucan phosphorylase, as well as the maltodextrin phosphorylases of bacteria. The members of this family catalyze the breakdown of oligosaccharides into glucose-1-phosphate units. They are important allosteric enzymes in carbohydrate metabolism. The allosteric control mechanisms of yeast and mammalian members of this family are different from that of bacterial members. The members of this family belong to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.

Carbohydrate phosphorylase. The members of this family catalyze the formation of glucose 1-phosphate from one of the following polyglucoses; glycogen, starch, glucan or maltodextrin.

glycogen phosphorylase; Provisional

Crystalstructure of human brain glycogen phosphorylase [Homo sapiens],5IKP_A Crystal structure of human brain glycogen phosphorylase bound to AMP [Homo sapiens]

ChainA, Glycogen phosphorylase, muscle form [Homo sapiens]

Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus]

Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus]

Crystalstructure of GPb in complex with DK10 [Oryctolagus cuniculus],4EKE_A Crystal structure of GPb in complex with DK11 [Oryctolagus cuniculus],4EKY_A Crystal structure of GPb in complex with DK15 [Oryctolagus cuniculus],4EL0_A Crystal structure of GPb in complex with DK16 [Oryctolagus cuniculus],4EL5_A Crystal structure of GPb in complex with DK12 [Oryctolagus cuniculus],4MHO_A Crystal structure of Gpb in complex with S3, SUGAR (N-[(BIPHENYL-4-YLOXY)ACETYL]-BETA-D-GLUCOPYRANOSYLAMINE) [Oryctolagus cuniculus],4MHS_A Crystal structure of Gpb in complex with SUGAR (N-[(2E)-3-(BIPHENYL-4-YL)PROP-2-ENOYL]-BETA-D-GLUCOPYRANOSYLAMINE [Oryctolagus cuniculus],4MI3_A Crystal structure of Gpb in complex with SUGAR (N-{(2R)-2-METHYL-3-[4-(PROPAN-2-YL)PHENYL]PROPANOYL}-BETA-D-GLUCOPYRANOSYLAMINE) (S21) [Oryctolagus cuniculus],4MI6_A Crystal structure of Gpb in complex with SUGAR (N-[4-(5,6,7,8-TETRAHYDRONAPHTHALEN-2-YL)BUTANOYL]-BETA-D-GLUCOPYRANOSYLAMINE) [Oryctolagus cuniculus],4MI9_A Crystal structure of Gpb in complex with SUGAR (N-[(3R)-3-(4-ETHYLPHENYL)BUTANOYL]-BETA-D-GLUCOPYRANOSYLAMINE) (S20) [Oryctolagus cuniculus],4MIC_A Crystal structure of Gpb in complex with SUGAR (N-{(2E)-3-[4-(PROPAN-2-YL)PHENYL]PROP-2-ENOYL}-BETA-D-GLUCOPYRANOSYLAMINE) (S6) [Oryctolagus cuniculus],4MRA_A Crystal structure of Gpb in complex with QUERCETIN [Oryctolagus cuniculus]

Glycogen phosphorylase OS=Bacillus subtilis (strain 168) OX=224308 GN=glgP PE=2 SV=1

Glycogen phosphorylase, brain form OS=Bos taurus OX=9913 GN=PYGB PE=2 SV=3

Glycogen phosphorylase OS=Chlamydia pneumoniae OX=83558 GN=glgP PE=3 SV=1

Glycogen phosphorylase, brain form OS=Pongo abelii OX=9601 GN=PYGB PE=2 SV=3

Glycogen phosphorylase, brain form (Fragment) OS=Rattus norvegicus OX=10116 GN=Pygb PE=1 SV=3