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 4.2.1.19), found at the N-terminal, dehydrated d-erythroimidazoleglycerolphosphate to imidazoleacetolphosphate, the latter function (EC 3.1.3.15), 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]
Reactions
edithisB-N
- D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate 3-(imidazol-4-yl)-2-oxopropyl phosphate H2O
hisB-C
- L-histidinol phosphate H2O L-histidinol phosphate
Non-fusion protein in other species
editHIS3 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).
References
edit- ^ Brilli, M.; Fani, R. (2004). "Molecular Evolution of hisB Genes". Journal of Molecular Evolution. 58 (2): 225–237. Bibcode:2004JMolE..58..225B. doi:10.1007/s00239-003-2547-x. PMID 15042344. S2CID 1684458.225-237&rft.date=2004&rft_id=info:doi/10.1007/s00239-003-2547-x&rft_id=https://api.semanticscholar.org/CorpusID:1684458#id-name=S2CID&rft_id=info:pmid/15042344&rft_id=info:bibcode/2004JMolE..58..225B&rft.aulast=Brilli&rft.aufirst=M.&rft.au=Fani, R.&rfr_id=info:sid/en.wikipedia.org:HisB" class="Z3988">
- ^ 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.
- ^ 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. doi:10.1128/jb.151.2.692-700.1982. PMC 220310. PMID 6284708.692-700&rft.date=1982&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC220310#id-name=PMC&rft_id=info:pmid/6284708&rft_id=info:doi/10.1128/jb.151.2.692-700.1982&rft.aulast=Grisolia&rft.aufirst=V.&rft.au=Carlomagno, M. S.&rft.au=Bruni, C. B.&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC220310&rfr_id=info:sid/en.wikipedia.org:HisB" class="Z3988">
- ^ 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. doi:10.1128/jb.155.3.1288-1296.1983. PMC 217827. PMID 6309747.1288-1296&rft.date=1983&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC217827#id-name=PMC&rft_id=info:pmid/6309747&rft_id=info:doi/10.1128/jb.155.3.1288-1296.1983&rft.aulast=Grisolia&rft.aufirst=V.&rft.au=Riccio, A.&rft.au=Bruni, C. B.&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC217827&rfr_id=info:sid/en.wikipedia.org:HisB" class="Z3988">
- ^ 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.D583 - D590&rft.date=2010&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3013716#id-name=PMC&rft_id=info:pmid/21097882&rft_id=info:doi/10.1093/nar/gkq1143&rft.aulast=Keseler&rft.aufirst=I. M.&rft.au=Collado-Vides, J.&rft.au=Santos-Zavaleta, A.&rft.au=Peralta-Gil, M.&rft.au=Gama-Castro, S.&rft.au=Muñiz-Rascado, L.&rft.au=Bonavides-Martinez, C.&rft.au=Paley, S.&rft.au=Krummenacker, M.&rft.au=Altman, T.&rft.au=Kaipa, P.&rft.au=Spaulding, A.&rft.au=Pacheco, J.&rft.au=Latendresse, M.&rft.au=Fulcher, C.&rft.au=Sarker, M.&rft.au=Shearer, A. G.&rft.au=MacKie, A.&rft.au=Paulsen, I.&rft.au=Gunsalus, R. P.&rft.au=Karp, P. D.&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3013716&rfr_id=info:sid/en.wikipedia.org:HisB" class="Z3988">
- ^ 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 16966333.37930-37941&rft.date=2006&rft_id=info:doi/10.1074/jbc.M604916200&rft_id=info:pmid/16966333&rft.aulast=Rangarajan&rft.aufirst=E. S.&rft.au=Proteau, A.&rft.au=Wagner, J.&rft.au=Hung, M. -N.&rft.au=Matte, A.&rft.au=Cygler, M.&rft_id=https://doi.org/10.1074%2Fjbc.M604916200&rfr_id=info:sid/en.wikipedia.org:HisB" class="Z3988">
- ^ 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. doi:10.1128/jb.174.11.3830-3831.1992. PMC 206079. PMID 1592835.3830-3831&rft.date=1992&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC206079#id-name=PMC&rft_id=info:pmid/1592835&rft_id=info:doi/10.1128/jb.174.11.3830-3831.1992&rft.aulast=Alifano&rft.aufirst=P.&rft.au=Carlomagno, M. S.&rft.au=Bruni, C. B.&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC206079&rfr_id=info:sid/en.wikipedia.org:HisB" class="Z3988">
- ^ 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 17884825.2716-2722&rft.date=2007&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2678898#id-name=PMC&rft_id=info:pmid/17884825&rft_id=info:doi/10.1093/molbev/msm204&rft.aulast=Patrick&rft.aufirst=W. M.&rft.au=Quandt, E. M.&rft.au=Swartzlander, D. B.&rft.au=Matsumura, I.&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2678898&rfr_id=info:sid/en.wikipedia.org:HisB" class="Z3988">
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