메뉴 건너뛰기




Volumn 180, Issue 6, 1998, Pages 1425-1430

A conserved histidine is essential for glycerolipid acyltransferase catalysis

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; GLYCEROL 3 PHOSPHATE ACYLTRANSFERASE; HISTIDINE; MUTANT PROTEIN;

EID: 0031941001     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.180.6.1425-1430.1998     Document Type: Article
Times cited : (135)

References (31)
  • 2
    • 0015994923 scopus 로고
    • Mutants of Escherichia coli defective in membrane phospholipid synthesis: Macromolecular synthesis in an sn-glycerol 3-phosphate acyltransferase Km mutant
    • Bell, R. M. 1974. Mutants of Escherichia coli defective in membrane phospholipid synthesis: macromolecular synthesis in an sn-glycerol 3-phosphate acyltransferase Km mutant. J. Bacteriol. 117:1065-1076.
    • (1974) J. Bacteriol. , vol.117 , pp. 1065-1076
    • Bell, R.M.1
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0028519115 scopus 로고
    • Isolation and characterisation of a maize cDNA that complements a 1-acyl sn-glycerol-3-phosphate acyltransferase mutant of Escherichia coli and encodes a protein which has similarities to other acyltransferases
    • Brown, A. P., J. Coleman, A. M. Tommey, M. D. Watson, and A. R. Slabas. 1994. Isolation and characterisation of a maize cDNA that complements a 1-acyl sn-glycerol-3-phosphate acyltransferase mutant of Escherichia coli and encodes a protein which has similarities to other acyltransferases. Plant Mol. Biol. 26:211-223.
    • (1994) Plant Mol. Biol. , vol.26 , pp. 211-223
    • Brown, A.P.1    Coleman, J.2    Tommey, A.M.3    Watson, M.D.4    Slabas, A.R.5
  • 6
    • 0024280501 scopus 로고
    • Dissecting the catalytic triad of a serine protease
    • Carter, P., and J. A. Wells. 1988. Dissecting the catalytic triad of a serine protease. Nature (London) 332:564-568.
    • (1988) Nature (London) , vol.332 , pp. 564-568
    • Carter, P.1    Wells, J.A.2
  • 7
    • 0023204278 scopus 로고
    • The catalytic role of the active site aspartic acid in serine proteases
    • Craik, C. S., S. Roczniak, C. Largman, and W. J. Rutter. 1987. The catalytic role of the active site aspartic acid in serine proteases. Science 237:909-913.
    • (1987) Science , vol.237 , pp. 909-913
    • Craik, C.S.1    Roczniak, S.2    Largman, C.3    Rutter, W.J.4
  • 8
    • 0016235686 scopus 로고
    • Mutants of Escherichia coli defective in membrane phospholipid synthesis: Mapping of sn-glycerol 3-phosphate acyltransferase Km mutants
    • Cronan, J. E., Jr., and R. M. Bell. 1974. Mutants of Escherichia coli defective in membrane phospholipid synthesis: mapping of sn-glycerol 3-phosphate acyltransferase Km mutants. J. Bacteriol. 120:227-233.
    • (1974) J. Bacteriol. , vol.120 , pp. 227-233
    • Cronan Jr., J.E.1    Bell, R.M.2
  • 9
    • 0001517649 scopus 로고    scopus 로고
    • Biosynthesis of membrane lipids
    • F. C. Neidhardt, R. Curtis, C. A. Gross, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), American Society for Microbiology, Washington, D.C
    • Cronan, J. E., Jr., and C. O. Rock. 1996. Biosynthesis of membrane lipids, p. 612-636. In F. C. Neidhardt, R. Curtis, C. A. Gross, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella typhimurium: cellular and molecular biology. American Society for Microbiology, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , pp. 612-636
    • Cronan Jr., J.E.1    Rock, C.O.2
  • 10
    • 0029153622 scopus 로고
    • A plant acyltransferase involved in triacylglycerol biosynthesis complements an Escherichia coli sn-1-acylglycerol-3-phosphate acyltransferase mutant
    • Hanke, C., F. P. Wolter, J. Coleman, G. Peterek, and M. Frentzen. 1995. A plant acyltransferase involved in triacylglycerol biosynthesis complements an Escherichia coli sn-1-acylglycerol-3-phosphate acyltransferase mutant. Eur. J. Biochem. 232:806-810.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 806-810
    • Hanke, C.1    Wolter, F.P.2    Coleman, J.3    Peterek, G.4    Frentzen, M.5
  • 11
    • 0019967636 scopus 로고
    • Synthesis of various phospholipids from 2-acyl lysophospholipids by Escherichia coli extract
    • Tokyo
    • Homma, H., and S. Nojima. 1982. Synthesis of various phospholipids from 2-acyl lysophospholipids by Escherichia coli extract. J. Biochem. (Tokyo) 91:1103-1110.
    • (1982) J. Biochem. , vol.91 , pp. 1103-1110
    • Homma, H.1    Nojima, S.2
  • 12
    • 0025900050 scopus 로고
    • Isolation and characterization of Escherichia coli K-12 mutants lacking both 2-acyl-glycerophosphoethanolamine acyltransferase and acyl-acyl carrier protein synthetase activity
    • Hsu, L., S. Jackowski, and C. O. Rock. 1991. Isolation and characterization of Escherichia coli K-12 mutants lacking both 2-acyl-glycerophosphoethanolamine acyltransferase and acyl-acyl carrier protein synthetase activity. J. Biol. Chem. 266:13783-13788.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13783-13788
    • Hsu, L.1    Jackowski, S.2    Rock, C.O.3
  • 13
    • 0024283581 scopus 로고
    • Cloning and nucleotide sequence of cDNA for the plastid glycerol-3-phosphate acyltransferase from squash
    • Ishizaki, O., I. Nishida, K. Agata, G. Eguchi, and N. Murata. 1988. Cloning and nucleotide sequence of cDNA for the plastid glycerol-3-phosphate acyltransferase from squash. FEBS Lett. 238:424-430.
    • (1988) FEBS Lett. , vol.238 , pp. 424-430
    • Ishizaki, O.1    Nishida, I.2    Agata, K.3    Eguchi, G.4    Murata, N.5
  • 14
    • 0028101325 scopus 로고
    • Sequence and function of the aas gene in Escherichia coli
    • Jackowski, S., P. D. Jackson, and C. O. Rock. 1994. Sequence and function of the aas gene in Escherichia coli. J. Biol. Chem. 269:2921-2928.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2921-2928
    • Jackowski, S.1    Jackson, P.D.2    Rock, C.O.3
  • 15
    • 0029411115 scopus 로고
    • Cloning of a coconut endosperm cDNA encoding a 1-acyl-sn-glycerol-3-phosphate acyltransferase that accepts medium-chain-length substrates
    • Knutzon, D. S., K. D. Lardizabal, J. S. Nelsen, J. L. Bleibaum, H. M. Davies, and J. G. Metz. 1995. Cloning of a coconut endosperm cDNA encoding a 1-acyl-sn-glycerol-3-phosphate acyltransferase that accepts medium-chain-length substrates. Plant Physiol. 109:999-1006.
    • (1995) Plant Physiol. , vol.109 , pp. 999-1006
    • Knutzon, D.S.1    Lardizabal, K.D.2    Nelsen, J.S.3    Bleibaum, J.L.4    Davies, H.M.5    Metz, J.G.6
  • 16
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, New York, N.Y
    • Miller, J. H. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, New York, N.Y.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 17
    • 0031028172 scopus 로고    scopus 로고
    • O-Acetyltransferases for chloramphenicol and other natural products
    • Murray, I. A., and W. V. Shaw. 1997. O-Acetyltransferases for chloramphenicol and other natural products. Antimicrob. Agents Chemother. 41:1-6.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 1-6
    • Murray, I.A.1    Shaw, W.V.2
  • 18
    • 0027438892 scopus 로고
    • A suppressor gene that enables Saccharomyces cerevisiae to grow without making sphingolipids encodes a protein that resembles an Escherichia coli fatty acyltransferase
    • Nagiec, M. M., G. B. Wells, R. L. Lester, and R. C. Dickson. 1993. A suppressor gene that enables Saccharomyces cerevisiae to grow without making sphingolipids encodes a protein that resembles an Escherichia coli fatty acyltransferase. J. Biol. Chem. 268:22156-22163.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22156-22163
    • Nagiec, M.M.1    Wells, G.B.2    Lester, R.L.3    Dickson, R.C.4
  • 19
    • 0016718568 scopus 로고
    • Acylation of sn-glycerol 3-phosphate in Escherichia coli: Study of the reaction with native palmitoyl-acyl carrier protein
    • Ray, T. K., and J. E. Cronan, Jr. 1975. Acylation of sn-glycerol 3-phosphate in Escherichia coli: study of the reaction with native palmitoyl-acyl carrier protein. J. Biol. Chem. 250:8422-8427.
    • (1975) J. Biol. Chem. , vol.250 , pp. 8422-8427
    • Ray, T.K.1    Cronan Jr., J.E.2
  • 20
    • 0030581109 scopus 로고    scopus 로고
    • Escherichia coli as a model for the regulation of dissociable (type II) fatty acid biosynthesis
    • Rock, C. O., and J. E. Cronan, Jr. 1996. Escherichia coli as a model for the regulation of dissociable (type II) fatty acid biosynthesis. Biochim. Biophys. Acta 1302:1-16.
    • (1996) Biochim. Biophys. Acta , vol.1302 , pp. 1-16
    • Rock, C.O.1    Cronan Jr., J.E.2
  • 21
    • 0018787017 scopus 로고
    • Preparative enzymatic synthesis and hydrophobic chromatography of acyl-acyl carrier protein
    • Rock, C. O., and J. L. Garwin. 1979. Preparative enzymatic synthesis and hydrophobic chromatography of acyl-acyl carrier protein. J. Biol. Chem. 254:7123-7128.
    • (1979) J. Biol. Chem. , vol.254 , pp. 7123-7128
    • Rock, C.O.1    Garwin, J.L.2
  • 22
    • 0019631120 scopus 로고
    • ATP stimulation of the sn-glycerol-3-phosphate acyltransferase of Escherichia coli
    • Rock, C. O., S. E. Goelz, and J. E. Cronan, Jr. 1981. ATP stimulation of the sn-glycerol-3-phosphate acyltransferase of Escherichia coli. Arch. Biochem. Biophys. 211:113-118.
    • (1981) Arch. Biochem. Biophys. , vol.211 , pp. 113-118
    • Rock, C.O.1    Goelz, S.E.2    Cronan Jr., J.E.3
  • 23
    • 0020351537 scopus 로고
    • Regulation of phospholipid synthesis in Escherichia coli. Composition of the acyl-acyl carrier protein pool in vivo
    • Rock, C. O., and S. Jackowski. 1982. Regulation of phospholipid synthesis in Escherichia coli. Composition of the acyl-acyl carrier protein pool in vivo. J. Biol. Chem. 257:10759-10765.
    • (1982) J. Biol. Chem. , vol.257 , pp. 10759-10765
    • Rock, C.O.1    Jackowski, S.2
  • 24
    • 0024364961 scopus 로고
    • Phospholipid dependence of homogeneous, reconstituted sn-glycerol-3-phosphate acyltransferase of Escherichia coli
    • Scheideler, M. A., and R. M. Bell. 1989. Phospholipid dependence of homogeneous, reconstituted sn-glycerol-3-phosphate acyltransferase of Escherichia coli. J. Biol. Chem. 264:12455-12461.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12455-12461
    • Scheideler, M.A.1    Bell, R.M.2
  • 25
    • 0026348480 scopus 로고
    • Characterization of active and latent forms of the membrane-associated sn-glycerol-3-phosphate acyltransferase of Escherichia coli
    • Scheideler, M. A., and R. M. Bell. 1991. Characterization of active and latent forms of the membrane-associated sn-glycerol-3-phosphate acyltransferase of Escherichia coli. J. Biol. Chem. 266:14321-14327.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14321-14327
    • Scheideler, M.A.1    Bell, R.M.2
  • 26
    • 0026432669 scopus 로고
    • Ser-His-Glu triad forms the catalytic site of the lipase from Geotrichum candidum
    • Schrag, J. D., Y. Li, S. Wu, and M. Cygler. 1991. Ser-His-Glu triad forms the catalytic site of the lipase from Geotrichum candidum. Nature (London) 351:761-764.
    • (1991) Nature (London) , vol.351 , pp. 761-764
    • Schrag, J.D.1    Li, Y.2    Wu, S.3    Cygler, M.4
  • 27
    • 0027383706 scopus 로고
    • Expression and identification of p90 as the murine mitochondrial glycerol-3-phosphate acyltransferase
    • Shaw-Fang, Y., S. Lee, Y. T. Hahm, and H. S. Sul. 1993. Expression and identification of p90 as the murine mitochondrial glycerol-3-phosphate acyltransferase. Biochemistry 32:9486-9491.
    • (1993) Biochemistry , vol.32 , pp. 9486-9491
    • Shaw-Fang, Y.1    Lee, S.2    Hahm, Y.T.3    Sul, H.S.4
  • 28
    • 0029007122 scopus 로고
    • A new family of lipolytic enzymes?
    • Upton, C., and J. T. Buckley. 1995. A new family of lipolytic enzymes? Trends Biochem. Sci. 20:178-179.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 178-179
    • Upton, C.1    Buckley, J.T.2
  • 29
    • 0026261717 scopus 로고
    • Purification and cDNA sequencing of an oleate selective acyl-ACP:sn-glycerol-3-phosphate acyltransferase from pea chloroplasts
    • Weber, S., F.-P. Wolter, F. Buck, M. Frentzen, and E. Heinz. 1991. Purification and cDNA sequencing of an oleate selective acyl-ACP:sn-glycerol-3-phosphate acyltransferase from pea chloroplasts. Plant Mol. Biol. 17:1067-1076.
    • (1991) Plant Mol. Biol. , vol.17 , pp. 1067-1076
    • Weber, S.1    Wolter, F.-P.2    Buck, F.3    Frentzen, M.4    Heinz, E.5
  • 30
  • 31
    • 0029079129 scopus 로고
    • Purification and reconstitution of murine mitochondrial glycerol-3-phosphate acyltransferase. Functional expression in baculovirus-infected insect cells
    • Yet, S.-F., Y. K. Moon, and H. S. Sul. 1995. Purification and reconstitution of murine mitochondrial glycerol-3-phosphate acyltransferase. Functional expression in baculovirus-infected insect cells. Biochemistry 34:7303-7310.
    • (1995) Biochemistry , vol.34 , pp. 7303-7310
    • Yet, S.-F.1    Moon, Y.K.2    Sul, H.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.