Characterization of ADP-Glucose Pyrophosphorylase from Rhodobacter sphaeroides 2.4.1: Evidence for the Involvement of Arginine in Allosteric Regulation

Identification of Functionally Important Amino-Terminal Arginines of Agrobacterium tumefaciens ADP-Glucose Pyrophosphorylase by Alanine Scanning Mutagenesis

“…Previous studies have probed the potential role of arginine(s) being involved in the binding of anionic substrate and effector molecules in various ADPGlc PPases ( − ). Further, arginine residues have been identified at or near highly conserved regions of the N-terminus ( , ).…”

“…Previous studies have probed the potential role of arginine(s) being involved in the binding of anionic substrate and effector molecules in various ADPGlc PPases ( − ). Further, arginine residues have been identified at or near highly conserved regions of the N-terminus ( , ). Although chemical modification experiments have indicated the importance of arginine residues in activity and regulation of ADPGlc PPase from E. coli (), Rhodobacter sphaeroides (), cyanobacteria ( , ), and spinach leaf (), only one study has revealed the function of a specific arginine.…”

Alteration of the substrate specificity of Thermus caldophilus ADP-glucose pyrophosphorylase by random mutagenesis through error-prone polymerase chain reaction

“…Likewise, phenylglyoxal-induced modification of the arginine residue decreased the AGPase activity from E. coli and spinach but increased that from T. caldophilus GK-24 [18,19,20,26]. For arginine residue-related activation, both the Agrobacterium tumefaciens enzyme [27] and the Rhodobacter sphaeroides enzyme [28] were known to be activated by modification with arginyl reagents, although the tendencies are depending on the assay conditions. In this study, error-prone PCR was performed to determine the amino acids involved in the substrate-specific AGPase activity by screening for UDP-glucose (UGPase) and UDP-GlcNAc pyrophosphorylase (UNGPase) activity.…”

Glucose-1-phosphate adenylyltransferase

“…; <28, 38, 39, 42, 57-61> no activation[13,22]; <4> recombinant enzyme is insensitive to 3-phosphoglycerate[53])[1-8, 10, 11, 13, 23-25, 27, 29, 32, 35, 37, 41, 43-45, 47, 48, 52, 53, 55, 56] 4-pyridoxic acid 5-phosphate <41> (<41> activation[32])[32] 6-phosphogluconate <58> (<58> slight activation[22])[22] ADP <4, 8, 11, 13, 18, 41> (<4, 8, 11, 13, 18, 41> activation, less effective than 3-phosphoglycerate [29]; <23, 25, 28, 38, 39, 42, 57-61> no activation [11, 13]) [29] AMP <4, 8, 11, 13, 18, 41, 115> (<4, 8, 11, 13, 18, 41> activation, less effective than 3-phosphoglycerate[29]; <115> activation at pH 7[49]; <23, 25, 28, 38, 39, 42, 57-61> no activation[11,13])[29,49] d-arabinitol 1,5-diphosphate <41> (<41> activation[32])[32] d-fructose 1,6-bisphosphate <2-47, 49, 51, 53, 54, 56-61, 114, 115, 117> (<11, 23, 25, 59> slight activation[3,4,11,23]; <11,13> activation of pyrophosphor-olysis[4][5][6];…”

“…22,32] NADPH <2-22, 24, 26-47, 49, 51, 53, 54, 56-61> (<19> activation, slight[10]; <19, 28, 36-42, 57-61> activation[10,13,30,22,32]; <39,42,57,61> one of the most effective activators[13]; <28,38> no activation[13]; <27-29,41> no ac-<2-47,49,51,53,54,56-61> activation[11,13,22,23,29,30,32]; <2-22,24,26-37,40,41,43-47,49,51,53,54,56,58-61> allosteric activator[22,32]; <34,58> influence on K m and pH-optimum[30]; <41> wild-type enzyme and mutant SG14[32]; <38,39,42,57,61> one of the most effective activators, less effective for Enterobacter hafniae[13]; <27-29> no activation[32])[11,13,22, 23, 29, 30, 32] pyruvate <30-33, 45-47, 49, 51, 53, 54, 56, 115> (<30-33,45-47,49,51,53,54,56> activation, kinetics[32]; <30,41> activation of chimeric enzyme EA contains the N-terminus of Escherichia coli enzyme and the C-terminus of Agrobacterium tumefaciens enzyme with higher affinity than activation of chimeric enzyme AE contains the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme[40]; <11,18,23,25,59> not[3,4,8,11,23])[32,40,49] …”