From Wikipedia, the free encyclopedia - View original article

Jump to: navigation, search

The hisB gene, found in the enterobacteria (such as E. coli), in Campylobacter jejuni and in Xylella/Xanthomonas encodes a protein involved in catalysis of two step in histidine biosynthesis (the sixth and eight step), namely the bifunctional Imidazoleglycerol-phosphate dehydratase/histidinol-phosphatase.[1]

The former function (EC, found at the N-terminal, dehydrated d-erythroimidazoleglycerolphosphate to imidazoleacetolphosphate, the latter function (EC, found at the C-terminal, dephosphorylates l-histidinolphosphate producing histidinol.[2][3][4]

The firth step is catalysed instead by histadinolphosphate aminotransferase (encoded by hisC)[5]

The peptide is 40.5kDa and associates to form a hexamer (unless truncated)[6]

In E. coli hisB is found on the hisGDCBHAFI operon[7]

The phosphatase activity possess a substrate ambiguity and overexpression of hisB can rescue phosphoserine phosphatase (serB) knockouts.[8]



D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate \rightleftharpoons 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O


L-histidinol phosphate + H2O \rightleftharpoons L-histidinol + phosphate

Non-fusion protein in other species[edit]

HIS3 from Saccharomyces cerevisiae is not a fused IGP dehydratase and hisidinol phosphatase, but an IGPD only (homologous to hisB-N). Whereas HIS2 is the HP (analogous to hisB-C, called hisJ in some prokaryotes).


  1. ^ Brilli, M.; Fani, R. (2004). "Molecular Evolution of hisB Genes". Journal of Molecular Evolution 58 (2): 225–237. doi:10.1007/s00239-003-2547-x. PMID 15042344.  edit
  2. ^ Parker95: Parker, A.R., Moore, J.A., Schwab, J.M., Davisson, V.J. (1995). "Escherichia coli Imidazoleglycerol Phosphate Dehydratase: Spectroscopic Characterization of the Enzymic Product and the Steric Course of the Reaction." Journal of the American Chemical Society.
  3. ^ Grisolia, V.; Carlomagno, M. S.; Bruni, C. B. (1982). "Cloning and expression of the distal portion of the histidine operon of Escherichia coli K-12". Journal of bacteriology 151 (2): 692–700. PMC 220310. PMID 6284708.  edit
  4. ^ Grisolia, V.; Riccio, A.; Bruni, C. B. (1983). "Structure and function of the internal promoter (hisBp) of the Escherichia coli K-12 histidine operon". Journal of bacteriology 155 (3): 1288–1296. PMC 217827. PMID 6309747.  edit
  5. ^ Keseler, I. M.; Collado-Vides, J.; Santos-Zavaleta, A.; Peralta-Gil, M.; Gama-Castro, S.; Muñiz-Rascado, L.; Bonavides-Martinez, C.; Paley, S.; Krummenacker, M.; Altman, T.; Kaipa, P.; Spaulding, A.; Pacheco, J.; Latendresse, M.; Fulcher, C.; Sarker, M.; Shearer, A. G.; MacKie, A.; Paulsen, I.; Gunsalus, R. P.; Karp, P. D. (2010). "EcoCyc: A comprehensive database of Escherichia coli biology". Nucleic Acids Research 39 (Database issue): D583–D590. doi:10.1093/nar/gkq1143. PMC 3013716. PMID 21097882.  edit
  6. ^ Rangarajan, E. S.; Proteau, A.; Wagner, J.; Hung, M. -N.; Matte, A.; Cygler, M. (2006). "Structural Snapshots of Escherichia coli Histidinol Phosphate Phosphatase along the Reaction Pathway". Journal of Biological Chemistry 281 (49): 37930–37941. doi:10.1074/jbc.M604916200. PMID 16966333.  edit
  7. ^ Alifano, P.; Carlomagno, M. S.; Bruni, C. B. (1992). "Location of the hisGDCBHAFI operon on the physical map of Escherichia coli". Journal of bacteriology 174 (11): 3830–3831. PMC 206079. PMID 1592835.  edit
  8. ^ Patrick, W. M.; Quandt, E. M.; Swartzlander, D. B.; Matsumura, I. (2007). "Multicopy Suppression Underpins Metabolic Evolvability". Molecular Biology and Evolution 24 (12): 2716–2722. doi:10.1093/molbev/msm204. PMC 2678898. PMID 17884825.  edit