EC Number |
General Information |
Reference |
---|
3.1.3.15 | evolution |
distribution of Cg0911 orthologues within bacteria, sequences and structure motifs comparisons, phylogenetic analysis, overview |
-, 750206 |
3.1.3.15 | evolution |
distribution of HisN orthologues within bacteria, sequences and structure motifs comparisons, phylogenetic analysis, overview |
-, 750206 |
3.1.3.15 | evolution |
enzyme Mtb HolPase belongs to the IMPase family, it is not an active inositol monophosphate phosphatase (IMPase) but a histidinol phosphate phosphatase (HolPase) |
-, 751106 |
3.1.3.15 | malfunction |
deletion of hisN in Corynebacterium glutamicum results in pronounced L-histidine bradytrophy instead of complete auxotrophy. Growth of the DELTAhisN mutant is visible after several days of incubation on minimal medium plates without L-histidine. Addition of L-histidine abolishes the observed growth defect completely. Complementation of the DELTAhisN growth defect is observed with gene cg0911 |
-, 750206 |
3.1.3.15 | malfunction |
deletion of the histidinol-phosphate phosphatase gene hisN results in histidine auxotrophy |
730327 |
3.1.3.15 | more |
importance of a highly conserved aspartate residue accompanied by several aromatic amino acid residues present in motif 5 for HolPase activity |
-, 750206 |
3.1.3.15 | more |
the cocrystal structure of Mtb HolPase with HOLP reveals a unique mode of substrate binding, a multizinc active-site pocket, and a product-exit channel. Dephosphorylation mechanism of Mtb Hol-Pase, overview |
-, 751106 |
3.1.3.15 | more |
the histidinol phosphate dephosphorylation reaction occurs at the interface between N- and C-terminal domains, structure-function relationship, active site structure with bound substrate, overview |
751088 |
3.1.3.15 | physiological function |
gene cg0911 encodes an enzyme with HolPase activity, the hisN paralogue gene cg0911 can complement the growth defect of mutant DELTAhisN. Enzyme Cg0911 is positively feedback regulated by L-histidinol |
-, 750206 |
3.1.3.15 | physiological function |
IMPase-like HPPs play a role only in His biosynthesis |
751088 |