Glucan phosphorylase [Carbohydrate transport and metabolism].

alpha-glucan phosphorylases. This family consists of known phosphorylases, and homologs believed to share the function of using inorganic phosphate to cleave an alpha 1,4 linkage between the terminal glucose residue and the rest of the polymer (maltodextrin, glycogen, etc.). The name of the glucose storage polymer substrate, and therefore the name of this enzyme, depends on the chain lengths and branching patterns. A number of the members of this family have been shown to operate on small maltodextrins, as may be obtained by utilization of exogenous sources. This family represents a distinct clade from the related family modeled by TIGR02093/pfam00343.

proteins similar to glycogen phosphorylase. This family is most closely related to the oligosaccharide phosphorylase domain family and other unidentified sequences. Oligosaccharide phosphorylase catalyzes the breakdown of oligosaccharides into glucose-1-phosphate units. They are important allosteric enzymes in carbohydrate metabolism.

Protein of unknown function (DUF3417). This family of proteins are functionally uncharacterized. This protein is found in bacteria and archaea. Proteins in this family are typically between 145 to 860 amino acids in length. This protein is found associated with pfam00343. This protein has a conserved AYF sequence motif.

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.

Starchphosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control. [Corynebacterium callunae],2C4M_B Starch phosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control. [Corynebacterium callunae],2C4M_C Starch phosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control. [Corynebacterium callunae],2C4M_D Starch phosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control. [Corynebacterium callunae]

ControlOf Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate [Oryctolagus cuniculus],1ABB_B Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate [Oryctolagus cuniculus],1ABB_C Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate [Oryctolagus cuniculus],1ABB_D Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate [Oryctolagus cuniculus]

IdentificationAnd Structural Characterization Of A Novel Allosteric Binding Site Of Glycogen Phosphorylase B [Oryctolagus cuniculus]

AmidocarbamateInhibitor Of Glycogen Phosphorylase [Oryctolagus cuniculus],1BX3_A Effects Of Commonly Used Cryoprotectants On Glycogen Phosphorylase Activity And Structure [Oryctolagus cuniculus],1C8K_A Flavopiridol Inhibits Glycogen Phosphorylase By Binding At The Inhibitor Site [Oryctolagus cuniculus],1FS4_A Structures of glycogen phosphorylase-inhibitor complexes and the implications for structure-based drug design [Oryctolagus cuniculus],1FTQ_A Structures Of Glycogen Phosphorylase-Inhibitor Complexes And The Implications For Structure-Based Drug Design [Oryctolagus cuniculus],1FTW_A Structures Of Glycogen Phosphorylase-Inhibitor Complexes And The Implications For Structure-Based Drug Design [Oryctolagus cuniculus],1FTY_A Structures Of Glycogen Phosphorylase-Inhibitor Complexes And The Implications For Structure-Based Drug Design [Oryctolagus cuniculus],1FU4_A Structures Of Glycogen Phosphorylase-Inhibitor Complexes And The Implications For Structure-Based Drug Design [Oryctolagus cuniculus],1FU7_A Structures Of Glycogen Phosphorylase-Inhibitor Complexes And The Implications For Structure-Based Drug Design [Oryctolagus cuniculus],1FU8_A Structures Of Glycogen Phosphorylase-Inhibitor Complexes And The Implications For Structure-Based Drug Design [Oryctolagus cuniculus],1GFZ_A Flavopiridol Inhibits Glycogen Phosphorylase By Binding At The Inhibitor Site [Oryctolagus cuniculus],1GG8_A Design Of Inhibitors Of Glycogen Phosphorylase: A Study Of Alpha-And Beta-C-Glucosides And 1-Thio-Beta-D-Glucose Compounds [Oryctolagus cuniculus],1GGN_A Structures of glycogen phosphorylase-inhibitor complexes and the implications for structure-based drug design [Oryctolagus cuniculus],1GPB_A GLYCOGEN PHOSPHORYLASE B: DESCRIPTION OF THE PROTEIN STRUCTURE [Oryctolagus cuniculus],1H5U_A THE 1.76 A RESOLUTION CRYSTAL STRUCTURE OF GLYCOGEN PHOSPHORYLASE B COMPLEXED WITH GLUCOSE AND CP320626, A POTENTIAL ANTIDIABETIC DRUG [Oryctolagus cuniculus],1HLF_A Binding Of Glucopyranosylidene-spiro-thiohydantoin To Glycogen Phosphorylase B: Kinetic And Crystallographic Stud [Oryctolagus cuniculus],1K06_A Crystallographic Binding Study of 100 mM N-benzoyl-N'-beta-D-glucopyranosyl urea to glycogen phosphorylase b [Oryctolagus cuniculus],1K08_A Crystallographic Binding Study of 10 mM N-benzoyl-N'-beta-D-glucopyranosyl urea to glycogen phosphorylase b [Oryctolagus cuniculus],1KTI_A Binding Of 100 Mm N-Acetyl-N'-Beta-D-Glucopyranosyl Urea To Glycogen Phosphorylase B: Kinetic And Crystallographic Studies [Oryctolagus cuniculus],1P29_A Crystal Structure of glycogen phosphorylase b in complex with maltopentaose [Oryctolagus cuniculus],1P2B_A Crystal Structure of Glycogen Phosphorylase B in Complex with Maltoheptaose [Oryctolagus cuniculus],1P2D_A Crystal Structure of Glycogen Phosphorylase B in complex with Beta Cyclodextrin [Oryctolagus cuniculus],1P2G_A Crystal Structure of Glycogen Phosphorylase B in complex with Gamma Cyclodextrin [Oryctolagus cuniculus],1P4G_A Crystal structure of glycogen phosphorylase b in complex with C-(1-azido-alpha-D-glucopyranosyl)formamide [Oryctolagus cuniculus],1P4H_A Crystal structure of glycogen phosphorylase b in complex with C-(1-acetamido-alpha-D-glucopyranosyl) formamide [Oryctolagus cuniculus],1P4J_A Crystal structure of glycogen phosphorylase b in complex with C-(1-hydroxy-beta-D-glucopyranosyl)formamide [Oryctolagus cuniculus],1WUT_A Acyl Ureas as Human Liver Glycogen Phosphorylase Inhibitors for the Treatment of Type 2 Diabetes [Oryctolagus cuniculus],1WUY_A Crystallographic studies on acyl ureas, a new class of inhibitors of glycogen phosphorylase. Broad specificity of the allosteric site [Oryctolagus cuniculus],1WV0_A Crystallographic studies on acyl ureas, a new class of inhibitors of glycogen phosphorylase. Broad specificity of the allosteric site [Oryctolagus cuniculus],1WV1_A Crystallographic studies on acyl ureas, a new class of inhibitors of glycogenphosphorylase. Broad specificity of the allosteric site [Oryctolagus cuniculus],1WW2_A Crystallographic studies on two bioisosteric analogues, N-acetyl-beta-D-glucopyranosylamine and N-trifluoroacetyl-beta-D-glucopyranosylamine, potent inhibitors of muscle glycogen phosphorylase [Oryctolagus cuniculus],1WW3_A Crystallographic studies on two bioisosteric analogues, N-acetyl-beta-D-glucopyranosylamine and N-trifluoroacetyl-beta-D-glucopyranosylamine, potent inhibitors of muscle glycogen phosphorylase [Oryctolagus cuniculus],2GPB_A COMPARISON OF THE BINDING OF GLUCOSE AND GLUCOSE-1-PHOSPHATE DERIVATIVES TO T-STATE GLYCOGEN PHOSPHORYLASE B [Oryctolagus cuniculus],2IEG_A Crystal structure of rabbit muscle glycogen phosphorylase in complex with 3,4-dihydro-2-quinolone [Oryctolagus cuniculus],2IEG_B Crystal structure of rabbit muscle glycogen phosphorylase in complex with 3,4-dihydro-2-quinolone [Oryctolagus cuniculus],2IEI_A Crystal structure of rabbit muscle glycogen phosphorylase in complex with 3,4-dihydro-2-quinolone [Oryctolagus cuniculus],2IEI_B Crystal structure of rabbit muscle glycogen phosphorylase in complex with 3,4-dihydro-2-quinolone [Oryctolagus cuniculus],2PRI_A BINDING OF 2-DEOXY-GLUCOSE-6-PHOSPHATE TO GLYCOGEN PHOSPHORYLASE B [Oryctolagus cuniculus],2PRJ_A Binding of N-acetyl-beta-D-glucopyranosylamine to Glycogen Phosphorylase B [Oryctolagus cuniculus],2QN7_A Glycogen Phosphorylase b in complex with N-4-hydroxybenzoyl-N'-4-beta-D-glucopyranosyl urea [Oryctolagus cuniculus],2QN8_A Glycogen Phosphorylase b in complex with N-4-nitrobenzoyl-N'-beta-D-glucopyranosyl urea [Oryctolagus cuniculus],2QN9_A Glycogen Phosphorylase in complex with N-4-aminobenzoyl-N'-beta-D-glucopyranosyl urea [Oryctolagus cuniculus],2SKC_A Pyridoxal Phosphorylase B In Complex With Fluorophosphate, Glucose And Inosine-5'-Monophosphate [Oryctolagus cuniculus],2SKD_A Pyridoxal Phosphorylase B In Complex With Phosphate, Glucose And Inosine-5'-Monophosphate [Oryctolagus cuniculus],2SKE_A Pyridoxal Phosphorylase B In Complex With Phosphite, Glucose And Inosine-5'-monophosphate [Oryctolagus cuniculus],3GPB_A COMPARISON OF THE BINDING OF GLUCOSE AND GLUCOSE-1-PHOSPHATE DERIVATIVES TO T-STATE GLYCOGEN PHOSPHORYLASE B [Oryctolagus cuniculus],4GPB_A COMPARISON OF THE BINDING OF GLUCOSE AND GLUCOSE-1-PHOSPHATE DERIVATIVES TO T-STATE GLYCOGEN PHOSPHORYLASE B [Oryctolagus cuniculus],5GPB_A COMPARISON OF THE BINDING OF GLUCOSE AND GLUCOSE-1-PHOSPHATE DERIVATIVES TO T-STATE GLYCOGEN PHOSPHORYLASE B [Oryctolagus cuniculus],6GPB_A REFINED CRYSTAL STRUCTURE OF THE PHOSPHORYLASE-HEPTULOSE 2-PHOSPHATE-OLIGOSACCHARIDE-AMP COMPLEX [Oryctolagus cuniculus],7GPB_A STRUCTURAL MECHANISM FOR GLYCOGEN PHOSPHORYLASE CONTROL BY PHOSPHORYLATION AND AMP [Oryctolagus cuniculus],7GPB_B STRUCTURAL MECHANISM FOR GLYCOGEN PHOSPHORYLASE CONTROL BY PHOSPHORYLATION AND AMP [Oryctolagus cuniculus],7GPB_C STRUCTURAL MECHANISM FOR GLYCOGEN PHOSPHORYLASE CONTROL BY PHOSPHORYLATION AND AMP [Oryctolagus cuniculus],7GPB_D STRUCTURAL MECHANISM FOR GLYCOGEN PHOSPHORYLASE CONTROL BY PHOSPHORYLATION AND AMP [Oryctolagus cuniculus],8GPB_A STRUCTURAL MECHANISM FOR GLYCOGEN PHOSPHORYLASE CONTROL BY PHOSPHORYLATION AND AMP [Oryctolagus cuniculus],9GPB_A THE ALLOSTERIC TRANSITION OF GLYCOGEN PHOSPHORYLASE [Oryctolagus cuniculus],9GPB_B THE ALLOSTERIC TRANSITION OF GLYCOGEN PHOSPHORYLASE [Oryctolagus cuniculus],9GPB_C THE ALLOSTERIC TRANSITION OF GLYCOGEN PHOSPHORYLASE [Oryctolagus cuniculus],9GPB_D THE ALLOSTERIC TRANSITION OF GLYCOGEN PHOSPHORYLASE [Oryctolagus cuniculus]

STRUCTURALMECHANISM FOR GLYCOGEN PHOSPHORYLASE CONTROL BY PHOSPHORYLATION AND AMP [Oryctolagus cuniculus],1GPA_B STRUCTURAL MECHANISM FOR GLYCOGEN PHOSPHORYLASE CONTROL BY PHOSPHORYLATION AND AMP [Oryctolagus cuniculus],1GPA_C STRUCTURAL MECHANISM FOR GLYCOGEN PHOSPHORYLASE CONTROL BY PHOSPHORYLATION AND AMP [Oryctolagus cuniculus],1GPA_D STRUCTURAL MECHANISM FOR GLYCOGEN PHOSPHORYLASE CONTROL BY PHOSPHORYLATION AND AMP [Oryctolagus cuniculus]

Maltodextrin phosphorylase OS=Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C) OX=523849 GN=malP PE=1 SV=1

Glycogen phosphorylase OS=Aquifex aeolicus (strain VF5) OX=224324 GN=glgP PE=3 SV=1

Glycogen phosphorylase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=glgP PE=1 SV=1

Glycogen phosphorylase OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) OX=233413 GN=glgP PE=3 SV=1

Glycogen phosphorylase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=glgP PE=3 SV=1