The enzyme works on a variety of alpha-D-aldose 1-phosphates and beta-L-aldose 1-phosphates (which have the same anomeric configuration as the former; see 2-Carb-6.2).
The enzyme works on a variety of alpha-D-aldose 1-phosphates and beta-L-aldose 1-phosphates (which have the same anomeric configuration as the former; see 2-Carb-6.2).
a bifunctional enzyme with phosphomannose isomerase (PMI), EC 5.3.1.8, and mannose-1-phosphate guanylyltransferase (Man-1-P GTase), EC 2.7.7.13, activities, which can synthesize GDP-mannose when accompanied by a phosphomannomutase/phosphoglucomutase (PMM/PGM) enzyme (PH0923). PH0925 protein is a thermostable enzyme with both PMI and multiple sugar-1-P NTase, cf. EC 2.7.7.37, activities. Substrate specificity of the sugar-1-P NTase activity of the PH0925 protein, overview
no activity with dATP, dCTP, and dTTP, and no activity with fructose-1-phosphate, alpha-D-galactose-1-phosphate, and N-acetyl-D-glucosamine-1-phosphate
the enzyme has multiple sugar-1-phosphate nucleotidylyltransferase, EC 2.7.7.37, and amino-sugar-1-phosphate acetyltransferase, EC 2.3.1.157, activities, overview. In addition to glucosamine-1-phosphate acetyltransferase activity, it possesses unique galactosamine-1-phosphate acetyltransferase activity, EC 2.7.7.83. Also, the enzyme possesses GlcNAc-1-phosphate nucleotidylyltransferase and N-acetyl-D-galactosamine-1-phosphate uridyltransferase, EC 2.7.7.23, activities, as well as the expected glucose-1-phosphate thymidylyltransferase, EC 2.7.7.24, activity
the enzyme has multiple sugar-1-phosphate nucleotidylyltransferase, EC 2.7.7.37, and amino-sugar-1-phosphate acetyltransferase, EC 2.3.1.157, activities, overview. In addition to glucosamine-1-phosphate acetyltransferase activity, it possesses unique galactosamine-1-phosphate acetyltransferase activity, EC 2.7.7.83. Also, the enzyme possesses GlcNAc-1-phosphate nucleotidylyltransferase and N-acetyl-D-galactosamine-1-phosphate uridyltransferase, EC 2.7.7.23, activities, as well as the expected glucose-1-phosphate thymidylyltransferase, EC 2.7.7.24, activity
a bifunctional enzyme with phosphomannose isomerase (PMI), EC 5.3.1.8, and mannose-1-phosphate guanylyltransferase (Man-1-P GTase), EC 2.7.7.13, activities, which can synthesize GDP-mannose when accompanied by a phosphomannomutase/phosphoglucomutase (PMM/PGM) enzyme (PH0923). PH0925 protein is a thermostable enzyme with both PMI and multiple sugar-1-P NTase, cf. EC 2.7.7.37, activities. Substrate specificity of the sugar-1-P NTase activity of the PH0925 protein, overview
the C-terminal 114 residue region of the PH0925 protein inhibits the Man-1-P GTase activity. The phosphomannose isomerase activity is abolished by deletion of the C-terminal 14 residues
the sugar-1-phosphate nucleotidylyltransferase activity is located in the region from the N-terminus to the 345th residue, the Man-1-P GTase activity is located in the C-terminal 114 residue region of the PH0925 protein, the phosphomannose isomerase requires the the C-terminal 14 residues
the C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form and, in turn, the high stability of the entire ST0452 protein
the C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form and, in turn, the high stability of the entire ST0452 protein
the C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form and, in turn, the high stability of the entire ST0452 protein
the enzyme contains the the N-terminal nucleotidylyltransferase domain (residues 1210) and the C-terminal acetyltransferase domain (residues 211401), respectively. Comparisons of the crystal structures of the ST0452 protein, PDB ID GGO, and Escherichia coli protein EcGlmU2, PDB ID 2OI5, comparison with ST0452 mutant enzymes, overview. Despite the structural similarities between the N- and C-termini of the ST0452 protein and those of Escherichia coli EcGlmU, the thermostabilities of the two proteins differ greatly, as EcGlmU is a mesophilic enzyme. The structures of these proteins do not correlate directly with their thermostability
the enzyme contains the the N-terminal nucleotidylyltransferase domain (residues 1210) and the C-terminal acetyltransferase domain (residues 211401), respectively. Comparisons of the crystal structures of the ST0452 protein, PDB ID GGO, and Escherichia coli protein EcGlmU2, PDB ID 2OI5, comparison with ST0452 mutant enzymes, overview. Despite the structural similarities between the N- and C-termini of the ST0452 protein and those of Escherichia coli EcGlmU, the thermostabilities of the two proteins differ greatly, as EcGlmU is a mesophilic enzyme. The structures of these proteins do not correlate directly with their thermostability
construction of expression vectors encoding a series of ST0452 C-terminal deletion mutants with hexahistidine tags at their C-termini, designated pST0452(DC005)H, pST0452(DC011)H, pST0452(DC021)H, pST0452(DC031)H, pST0452(DC041) H, pST0452(DC051)H, pST0452(DC071)H, pST0452 (DC121)H and pST0452(DC171)H. The deletion mutants retain the same tertiary structures as the wild-type ST0452 protein
construction of expression vectors encoding a series of ST0452 C-terminal deletion mutants with hexahistidine tags at their C-termini, designated pST0452(DC005)H, pST0452(DC011)H, pST0452(DC021)H, pST0452(DC031)H, pST0452(DC041) H, pST0452(DC051)H, pST0452(DC071)H, pST0452 (DC121)H and pST0452(DC171)H. The deletion mutants retain the same tertiary structures as the wild-type ST0452 protein
site-directed mutagenesis of the active site results in 11 mutants, five of which sows increased kcat and Km values, but also increased activity compared to the wild-type, all mutants show the same thermostability as the wild-type
site-directed mutagenesis of the active site results in 11 mutants, five of which sows increased kcat and Km values, but also increased activity compared to the wild-type, all mutants show the same thermostability as the wild-type
Akutsu, J.; Zhang, Z.; Morita, R.; Kawarabayasi, Y.
Identification and characterization of a thermostable bifunctional enzyme with phosphomannose isomerase and sugar-1-phosphate nucleotidylyltransferase activities from a hyperthermophilic archaeon, Pyrococcus horikoshii OT3