EC Number   |
General Information |
Reference |
|---|
    2.7.1.33 | evolution |
comparison of MtPanK with the Escherichia coli enzyme EcPanK, overview. Despite the high sequence identity (52%) between EcPanK and MtPanK, the two enzymes differ in many respects, crystal structure comparison. While EcPanK is specific for ATP, MtPanK exhibits dual specificity and can make use of ATP as well as GTP for phosphorylating pantothenic acid. CoA binds nearly 40% more tightly to MtPanK than to EcPanK |
-, 758598 |
| 2.7.1.33 | evolution |
isozyme PANK3 belongs to the ASKHA kinase superfamily, which typically uses either an Asp or Glu residue as the catalytic base to activate the substrate hydroxyl for attack on the gamma-phosphate of ATP |
759477 |
| 2.7.1.33 | evolution |
isozyme PANK3 belongs to the ASKHA kinase superfamily, which typically uses either an Asp or Glu residue as the catalytic base to activate the substrate hydroxyl for attack on the gamma-phosphate of ATP. Glu138 appears to be the logical candidate for the catalytic base |
759477 |
| 2.7.1.33 | evolution |
the human genome encodes three well-characterized and nearly identical pantothenate kinases (PANK1-3) plus a putative bifunctional protein (PANK4) with a predicted amino-terminal pantothenate kinase domain fused to a carboxy-terminal phosphatase domain. Structural and phylogenetic analyses show that all active, characterized PANKs contain the key catalytic residues Glu138 and Arg207 (HsPANK3 numbering). All amniote PANK4s, including human PANK4, encode Glu138Val and Arg207Trp substitutions which are predicted to inactivate kinase activity. Human PANK4 is a pseudo-pantothenate kinase, a catalytically deficient variant of the catalytically active PANK4 found in plants and fungi. Evolutionary history of PANK, phylogenetic analysis, overview |
760099 |
| 2.7.1.33 | evolution |
the human genome encodes three well-characterized and nearly identical pantothenate kinases (PANK1-3) plus a putative bifunctional protein (PANK4) with a predicted N-terminal pantothenate kinase domain fused to a C-terminal phosphatase domain. Structural and phylogenetic analyses show that all active, characterized PANKs contain the key catalytic residues Glu138 and Arg207 (HsPANK3 numbering). All amniote PANK4s, including human PANK4, encode Glu138Val and Arg207Trp substitutions which are predicted to inactivate kinase activity. Human PANK4 is a pseudo-pantothenate kinase, a catalytically deficient variant of the catalytically active PANK4 found in plants and fungi. Evolutionary history of PANK, overview |
760099 |
| 2.7.1.33 | malfunction |
altered pantothenate utilization dramatically alters the susceptibility of yeast cells to ergosterol biosynthesis inhibitors. Inhibition of pantothenic acid utilization synergizes with the activity of the ergosterol molecule-targeting antifungal amphotericin B and antagonizes that of the ergosterol pathway-targeting antifungal drug terbinafine. Inhibition of pantothenate utilization results in reduced susceptibility to terbinafine and enhanced susceptibility to amphotericin B. Inhibition of Cab1p activity results in reduced squalene and lanosterol levels |
-, 759494 |
| 2.7.1.33 | malfunction |
disease: pantothenate kinase-associated neurodegeneration |
703958 |
| 2.7.1.33 | malfunction |
epigenetic gene silencing of PanK resulting in a significant reduction of PanK activity, intracellular CoA concentrations, and growth retardation in vitro, reinforcing the importance of this gene in Entamoeba histolytica |
759375 |
| 2.7.1.33 | malfunction |
flies carrying a fumble loss-of-function allele have a 3fold increase in total zinc levels per dry weight when compared to control strains, but no change in total iron, copper or manganese levels |
722262 |
| 2.7.1.33 | malfunction |
human PANK3 is inactivated by mutations Glu138Val and Arg207Trp |
760099 |
