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Volumn 379, Issue 2, 2004, Pages 253-261

Mapping of catalytically important residues in the rat L-histidine decarboxylase enzyme using bioinformatic and site-directed mutagenesis approaches

Author keywords

Histamine; Histidine decarboxylase (HDC); L amino acid decarboxylase; Site directed mutagenesis

Indexed keywords

AMINES; BIOSYNTHESIS; CARBOXYLIC ACIDS; ENZYMES; LIVING SYSTEMS STUDIES; MUTAGENESIS; PROTEINS; VITAMINS;

EID: 2342582122     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20031525     Document Type: Article
Times cited : (28)

References (32)
  • 1
    • 0018066295 scopus 로고
    • Histamine: Its role in physiological and pathological processes
    • Beaven, M. A. (1978) Histamine: Its role in physiological and pathological processes. Monogr. Allergy 13, 1-113
    • (1978) Monogr. Allergy , vol.13 , pp. 1-113
    • Beaven, M.A.1
  • 3
    • 0038240071 scopus 로고    scopus 로고
    • New functions of histamine found in histidine decarboxylase gene knockout mice
    • Ohtsu, H. and Watanabe, T. (2003) New functions of histamine found in histidine decarboxylase gene knockout mice. Biochem. Biophys. Res. Commun. 305, 443-447
    • (2003) Biochem. Biophys. Res. Commun. , vol.305 , pp. 443-447
    • Ohtsu, H.1    Watanabe, T.2
  • 4
    • 0029954598 scopus 로고    scopus 로고
    • Experimental evidence for structure-activity features in common between mammalian histidine decarboxylase and ornithine decarboxylase
    • Engel, N., Olmo, M. T., Coleman, C. S., Medina, M. A., Pegg, A. E. and Sanchez-Jimenez, F. (1996) Experimental evidence for structure-activity features in common between mammalian histidine decarboxylase and ornithine decarboxylase. Biochem. J. 320, 365-368
    • (1996) Biochem. J. , vol.320 , pp. 365-368
    • Engel, N.1    Olmo, M.T.2    Coleman, C.S.3    Medina, M.A.4    Pegg, A.E.5    Sanchez-Jimenez, F.6
  • 5
    • 0034043406 scopus 로고    scopus 로고
    • Amino- and carboxy-terminal PEST domains mediate gastrin stabilization of rat L-histidine decarboxylase isoforms
    • Fleming, J. V. and Wang, T. C. (2000) Amino- and carboxy-terminal PEST domains mediate gastrin stabilization of rat L-histidine decarboxylase isoforms. Mol. Cell. Biol. 20, 4932-4947
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 4932-4947
    • Fleming, J.V.1    Wang, T.C.2
  • 6
    • 0030778610 scopus 로고    scopus 로고
    • Degradation of the 74 kDa form of L-histidine decarboxylase via the ubiquitin-proteasome pathway in a rat basophilic/mast cell line (RBL-2H3)
    • Tanaka, S., Nemoto, K., Yamamura, E., Ohmura, S. and Ichikawa, A. (1997) Degradation of the 74 kDa form of L-histidine decarboxylase via the ubiquitin-proteasome pathway in a rat basophilic/mast cell line (RBL-2H3). FEBS Lett. 417, 203-207
    • (1997) FEBS Lett. , vol.417 , pp. 203-207
    • Tanaka, S.1    Nemoto, K.2    Yamamura, E.3    Ohmura, S.4    Ichikawa, A.5
  • 7
    • 0019498993 scopus 로고
    • Histidine decarboxylase. Purification from fetal rat liver, immunologic properties, and histochemical localization in brain and stomach
    • Tran, V. and Snyder, S. (1981) Histidine decarboxylase. Purification from fetal rat liver, immunologic properties, and histochemical localization in brain and stomach. J. Biol. Chem. 256, 680-686
    • (1981) J. Biol. Chem. , vol.256 , pp. 680-686
    • Tran, V.1    Snyder, S.2
  • 8
    • 0021143815 scopus 로고
    • Histidine decarboxylase: Isolation and molecular characteristics
    • Grzanna, R. (1984) Histidine decarboxylase: isolation and molecular characteristics. Neurochem. Res. 9, 993-1009
    • (1984) Neurochem. Res. , vol.9 , pp. 993-1009
    • Grzanna, R.1
  • 9
    • 0022465763 scopus 로고
    • Purification and characterization of histidine decarboxylase from mouse kidney
    • Martin, S. A. and Bishop, J. O. (1986) Purification and characterization of histidine decarboxylase from mouse kidney. Biochem. J. 234, 349-354
    • (1986) Biochem. J. , vol.234 , pp. 349-354
    • Martin, S.A.1    Bishop, J.O.2
  • 10
    • 0033036614 scopus 로고    scopus 로고
    • Histidine decarboxylase in rat stomach ECL cells: Relationship between enzyme activity and different molecular forms
    • Dartsch, C., Chen, D., Hakanson, R. and Persson, L. (1999) Histidine decarboxylase in rat stomach ECL cells: relationship between enzyme activity and different molecular forms. Regul. Pept. 81, 41-48
    • (1999) Regul. Pept. , vol.81 , pp. 41-48
    • Dartsch, C.1    Chen, D.2    Hakanson, R.3    Persson, L.4
  • 11
    • 0025312902 scopus 로고
    • Purification and characterization of L-histidine decarboxylase from mouse mastocytoma P-815 cells
    • Tokyo
    • Ohmori, E., Fukui, T., Imanishi, N., Yatsunami, K. and Ichikawa, A. (1990) Purification and characterization of L-histidine decarboxylase from mouse mastocytoma P-815 cells. J. Biochem. (Tokyo) 107, 834-839
    • (1990) J. Biochem. , vol.107 , pp. 834-839
    • Ohmori, E.1    Fukui, T.2    Imanishi, N.3    Yatsunami, K.4    Ichikawa, A.5
  • 12
    • 0020123673 scopus 로고
    • Properties of histidine decarboxylase from rat gastric mucosa
    • Savany, A. and Cronenberger, L. (1982) Properties of histidine decarboxylase from rat gastric mucosa. Eur. J. Biochem. 123, 593-599
    • (1982) Eur. J. Biochem. , vol.123 , pp. 593-599
    • Savany, A.1    Cronenberger, L.2
  • 13
    • 0020470932 scopus 로고
    • Isolation and properties of multiple forms of histidine decarboxylase from rat gastric mucosa
    • Savany, A. and Cronenberger, L. (1982) Isolation and properties of multiple forms of histidine decarboxylase from rat gastric mucosa. Biochem. J. 205, 405-412
    • (1982) Biochem. J. , vol.205 , pp. 405-412
    • Savany, A.1    Cronenberger, L.2
  • 14
    • 0037414776 scopus 로고    scopus 로고
    • The production of 53-55 kDa isoforms is not required for rat I-histidine decarboxylase activity
    • Fleming, J. V. and Wang, T. C. (2003) The production of 53-55 kDa isoforms is not required for rat I-histidine decarboxylase activity. J. Biol. Chem. 278, 686-694
    • (2003) J. Biol. Chem. , vol.278 , pp. 686-694
    • Fleming, J.V.1    Wang, T.C.2
  • 15
    • 0036737948 scopus 로고    scopus 로고
    • Spectroscopic analysis of recombinant rat histidine decarboxylase
    • Tokyo
    • Olmo, M. T., Sanchez-Jimenez, F., Medina, M. A. and Hayashi, H. (2002) Spectroscopic analysis of recombinant rat histidine decarboxylase. J. Biochem. (Tokyo) 132, 433-439
    • (2002) J. Biochem. , vol.132 , pp. 433-439
    • Olmo, M.T.1    Sanchez-Jimenez, F.2    Medina, M.A.3    Hayashi, H.4
  • 16
    • 0028281750 scopus 로고
    • Multiple evolutionary origin of pyridoxal-5′-phosphate-dependent amino acid decarboxylases
    • Sandmeier, E., Hale, T. I. and Christen, P. (1994) Multiple evolutionary origin of pyridoxal-5′-phosphate-dependent amino acid decarboxylases. Eur. J. Biochem. 221, 997-1002
    • (1994) Eur. J. Biochem. , vol.221 , pp. 997-1002
    • Sandmeier, E.1    Hale, T.I.2    Christen, P.3
  • 17
    • 0035755593 scopus 로고    scopus 로고
    • From cofactor to enzymes. The molecular evolution of pyridoxal-5′- phosphate-dependent enzymes
    • Christen, P. and Mehta, P. K. (2001) From cofactor to enzymes. The molecular evolution of pyridoxal-5′-phosphate-dependent enzymes. Chem. Rec. 1, 436-447
    • (2001) Chem. Rec. , vol.1 , pp. 436-447
    • Christen, P.1    Mehta, P.K.2
  • 18
    • 0032444219 scopus 로고    scopus 로고
    • Structure, evolution and action of vitamin B6-dependent enzymes
    • Jansonius, J. N. (1998) Structure, evolution and action of vitamin B6-dependent enzymes. Curr. Opin. Struct. Biol. 8, 759-769
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 759-769
    • Jansonius, J.N.1
  • 19
    • 0028921425 scopus 로고
    • Structural motifs for pyridoxal-5′-phosphate binding in decarboxylases: An analysis based on the crystal structure of the Lactobacillus 30a ornithine decarboxylase
    • Momany, C., Ghosh, R. and Hackert, M. L. (1995) Structural motifs for pyridoxal-5′-phosphate binding in decarboxylases: an analysis based on the crystal structure of the Lactobacillus 30a ornithine decarboxylase. Protein Sci. 5, 849-854
    • (1995) Protein Sci. , vol.5 , pp. 849-854
    • Momany, C.1    Ghosh, R.2    Hackert, M.L.3
  • 20
    • 0031863617 scopus 로고    scopus 로고
    • Motifs and structural fold of the cofactor binding site of human glutamate decarboxylase
    • Qu, K., Martin, D. L. and Lawrence, C. E. (1998) Motifs and structural fold of the cofactor binding site of human glutamate decarboxylase. Protein Sci. 7, 1092-1105
    • (1998) Protein Sci. , vol.7 , pp. 1092-1105
    • Qu, K.1    Martin, D.L.2    Lawrence, C.E.3
  • 22
    • 0032456134 scopus 로고    scopus 로고
    • Aromatic L-amino acid decarboxylase: Conformational change in the flexible region around Arg334 is required during the transaldimination process
    • Ishii, S., Hayashi, H., Okamoto, A. and Kagamiyama, H. (1998) Aromatic L-amino acid decarboxylase: conformational change in the flexible region around Arg334 is required during the transaldimination process. Protein Sci. 7, 1802-1810
    • (1998) Protein Sci. , vol.7 , pp. 1802-1810
    • Ishii, S.1    Hayashi, H.2    Okamoto, A.3    Kagamiyama, H.4
  • 23
    • 0032538322 scopus 로고    scopus 로고
    • Multiple forms of rat stomach hlstidine decarboxylase may reflect posttranslational activation of the enzyme
    • Dartsch, C., Chen, D. and Persson, L. (1998) Multiple forms of rat stomach hlstidine decarboxylase may reflect posttranslational activation of the enzyme. Regul. Pept. 77, 33-41
    • (1998) Regul. Pept. , vol.77 , pp. 33-41
    • Dartsch, C.1    Chen, D.2    Persson, L.3
  • 24
    • 0029090374 scopus 로고
    • Pyridoxal enzymes: Mechanistic diversity and uniformity
    • Tokyo
    • Hayashi, H. (1995) Pyridoxal enzymes: mechanistic diversity and uniformity. J. Biochem. (Tokyo) 118, 463-473
    • (1995) J. Biochem. , vol.118 , pp. 463-473
    • Hayashi, H.1
  • 26
    • 0030822249 scopus 로고    scopus 로고
    • Mutation of cysteine 111 in DOPA decarboxylase leads to active site perturbation
    • Dominici, P., Moore, P. S., Castellani, S., Bertoldi, M. and Voltattorni, C. B. (1997) Mutation of cysteine 111 in DOPA decarboxylase leads to active site perturbation. Protein Sci. 6, 2007-2015
    • (1997) Protein Sci. , vol.6 , pp. 2007-2015
    • Dominici, P.1    Moore, P.S.2    Castellani, S.3    Bertoldi, M.4    Voltattorni, C.B.5
  • 27
    • 0018878548 scopus 로고
    • Mammalian histidine decarboxylase; changes in molecular properties induced by oxidation and reduction
    • Hammar, L. and Hjerten, S. (1980) Mammalian histidine decarboxylase; changes in molecular properties induced by oxidation and reduction. Agents Actions 10, 93-98
    • (1980) Agents Actions , vol.10 , pp. 93-98
    • Hammar, L.1    Hjerten, S.2
  • 28
    • 0027965970 scopus 로고
    • Rapid exchange of subunits of mammalian ornithine decarboxylase
    • Coleman, C. S., Stanley, B. A., Viswanath, R. and Pegg, A. E. (1994) Rapid exchange of subunits of mammalian ornithine decarboxylase. J. Biol. Chem. 269, 3155-3158
    • (1994) J. Biol. Chem. , vol.269 , pp. 3155-3158
    • Coleman, C.S.1    Stanley, B.A.2    Viswanath, R.3    Pegg, A.E.4
  • 29
    • 0345712325 scopus 로고    scopus 로고
    • The pest regions containing C-termini of mammalian ornithine decarboxylase and histidine decarboxylase play different roles in protein degradation
    • Olmo, M. T., Rodriguez-Agudo, D., Medina, M. A. and Sanchez-Jimenez, F. (1999) The pest regions containing C-termini of mammalian ornithine decarboxylase and histidine decarboxylase play different roles in protein degradation. Biochem. Biophys. Res. Commun. 257, 269-272
    • (1999) Biochem. Biophys. Res. Commun. , vol.257 , pp. 269-272
    • Olmo, M.T.1    Rodriguez-Agudo, D.2    Medina, M.A.3    Sanchez-Jimenez, F.4
  • 31
    • 0034826435 scopus 로고    scopus 로고
    • Mutation of residues in the coenzyme binding pocket of Dopa decarboxylase. Effects on catalytic properties
    • Bertoldi, M., Castellani, S. and Bori Voltattomi, C. (2001) Mutation of residues in the coenzyme binding pocket of Dopa decarboxylase. Effects on catalytic properties. Eur. J. Biochem. 268, 2975-2981
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2975-2981
    • Bertoldi, M.1    Castellani, S.2    Bori Voltattomi, C.3
  • 32
    • 0021322926 scopus 로고
    • Purification of histidine decarboxylase from the liver of fetal rats and its immunochemical and immunohistochemical characterization
    • Taguchi, Y., Watanabe, T., Kubota, H., Hayashi, H. and Wada, H. (1984) Purification of histidine decarboxylase from the liver of fetal rats and its immunochemical and immunohistochemical characterization. J. Biol. Chem. 259, 5214-5221
    • (1984) J. Biol. Chem. , vol.259 , pp. 5214-5221
    • Taguchi, Y.1    Watanabe, T.2    Kubota, H.3    Hayashi, H.4    Wada, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.