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Volumn 3, Issue , 2003, Pages 1-10

Molecular cloning and characterization of Escherichia coli K12 ygjG gene

Author keywords

[No Author keywords available]

Indexed keywords

2 OXOGLUTARIC ACID; AMINOTRANSFERASE; BACTERIAL ENZYME; CADAVERINE; DNA FRAGMENT; MESSENGER RNA; NUCLEIC ACID BASE; PUTRESCINE; PUTRESCINE:2 OXOGLUTARIC ACID AMINOTRANSFERASE; SPERMIDINE; UNCLASSIFIED DRUG; DIAMINE AMINOTRANSFERASE; ESCHERICHIA COLI PROTEIN; PRIMER DNA; RECOMBINANT PROTEIN; YGJG PROTEIN, E COLI;

EID: 2942748534     PISSN: 14712180     EISSN: 14712180     Source Type: Journal    
DOI: 10.1186/1471-2180-3-2     Document Type: Article
Times cited : (53)

References (33)
  • 1
    • 0022450919 scopus 로고
    • Recent advances in the biochemistry of polyamines in eukaryotes
    • Pegg AE Recent advances in the biochemistry of polyamines in eukaryotes. Biochem J 1986, 234:249-262
    • (1986) Biochem J , vol.234 , pp. 249-262
    • Pegg, A.E.1
  • 2
    • 0022001625 scopus 로고
    • Polyamines in microorganisms
    • Tabor CW and Tabor H Polyamines in microorganisms. Microbiol Rev 1985, 49:81-99
    • (1985) Microbiol Rev , vol.49 , pp. 81-99
    • Tabor, C.W.1    Tabor, H.2
  • 3
    • 0014295537 scopus 로고
    • Studies on DNA-dependent RNA polymerase from Escherichia coli. I. The mechanism of polyamine induced stimulation of enzyme activity
    • Abraham KA Studies on DNA-dependent RNA polymerase from Escherichia coli. I. The mechanism of polyamine induced stimulation of enzyme activity. Eur J Biochem 1968, 5:143-146
    • (1968) Eur J Biochem , vol.5 , pp. 143-146
    • Abraham, K.A.1
  • 5
    • 0025294783 scopus 로고
    • Transcriptional effects of polyamines on ribosomal proteins and on polyamine-synthesizing enzymes in Escherichia coli
    • Huang S, Panagiotidis CA and Canellakis ES Transcriptional effects of polyamines on ribosomal proteins and on polyamine-synthesizing enzymes in Escherichia coli. Proc Natl Acad Sci USA 1990, 87:3464-3468
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 3464-3468
    • Huang, S.1    Panagiotidis, C.A.2    Canellakis, E.S.3
  • 6
    • 0027420797 scopus 로고
    • Correlation between the inhibition of cell growth by accumulated polyamines and the decrease of magnesium and ATP
    • He Y, Kashiwagi K, Fukuchi J, Terao K, Shirahata A and Igarashi K Correlation between the inhibition of cell growth by accumulated polyamines and the decrease of magnesium and ATP. Eur J Biochem 1993, 217:89-96
    • (1993) Eur J Biochem , vol.217 , pp. 89-96
    • He, Y.1    Kashiwagi, K.2    Fukuchi, J.3    Terao, K.4    Shirahata, A.5    Igarashi, K.6
  • 7
    • 0023881236 scopus 로고
    • Polyamine metabolism and its importance in neoplastic growth and a target for chemotherapy
    • Pegg AE Polyamine metabolism and its importance in neoplastic growth and a target for chemotherapy. Cancer Res 1988, 48:759-774
    • (1988) Cancer Res , vol.48 , pp. 759-774
    • Pegg, A.E.1
  • 8
    • 0026877727 scopus 로고
    • Enzymes and pathways of polyamine breakdown in microorganisms
    • Large PJ Enzymes and pathways of polyamine breakdown in microorganisms. FEMS Microbiol Rev 1992, 88:249-262
    • (1992) FEMS Microbiol Rev , vol.88 , pp. 249-262
    • Large, P.J.1
  • 9
    • 0028070407 scopus 로고
    • Propeties and structure of spermidine acetyltransferase in Escherichia coli
    • Fukuchi J, Kashiwagi K, Takio K and Igarashi K Propeties and structure of spermidine acetyltransferase in Escherichia coli. J Biol Chem 1994, 269:22581-22585
    • (1994) J Biol Chem , vol.269 , pp. 22581-22585
    • Fukuchi, J.1    Kashiwagi, K.2    Takio, K.3    Igarashi, K.4
  • 12
    • 2942720171 scopus 로고
    • Purification and properties of a diamine α-ketoglutarate transaminase from Escherichia coli
    • Kim KH Purification and properties of a diamine α-ketoglutarate transaminase from Escherichia coli. J Biol Chem 1964, 239:783-786
    • (1964) J Biol Chem , vol.239 , pp. 783-786
    • Kim, K.H.1
  • 13
    • 0036299634 scopus 로고    scopus 로고
    • Functional analysis and regulation of the divergent spuABCDEFGH-spul operons for polyamine uptake and utilization in Pseudomonas aeruginosa PAOI
    • Lu CD, Itoh Y, Nakada Y and Jiang Y Functional analysis and regulation of the divergent spuABCDEFGH-spul operons for polyamine uptake and utilization in Pseudomonas aeruginosa PAOI. J Bacteriol 2002, 184:3765-3773
    • (2002) J Bacteriol , vol.184 , pp. 3765-3773
    • Lu, C.D.1    Itoh, Y.2    Nakada, Y.3    Jiang, Y.4
  • 14
    • 0030800296 scopus 로고    scopus 로고
    • Purification and characterization of polyamine aminotransferase of Arthrobacter sp. TMP-1
    • Yorifuji T, Kondo S, Shimizu E, Naka T and Ishihara T Purification and characterization of polyamine aminotransferase of Arthrobacter sp. TMP-1. J Biochem (Tokyo) 1997, 122:537-543
    • (1997) J Biochem (Tokyo) , vol.122 , pp. 537-543
    • Yorifuji, T.1    Kondo, S.2    Shimizu, E.3    Naka, T.4    Ishihara, T.5
  • 15
    • 0022390872 scopus 로고
    • Metabolic pathway for the utilization of L-arginine, L-ornithine, agmathine, and putrescine as nitrogen sources in Escherichia coli K-12
    • Snaibe E, Metzer E and Halpern YS Metabolic pathway for the utilization of L-arginine, L-ornithine, agmathine, and putrescine as nitrogen sources in Escherichia coli K-12. J Bacteriol 1985, 163:933-937
    • (1985) J Bacteriol , vol.163 , pp. 933-937
    • Snaibe, E.1    Metzer, E.2    Halpern, Y.S.3
  • 16
    • 0000590571 scopus 로고
    • Pyrrolidine and putrscine metabolism: γ-Aminobuyraldehyde dehydrogenase
    • Jakoby WB and Fredericks J Pyrrolidine and putrscine metabolism: γ-aminobuyraldehyde dehydrogenase. J Biol Chem 1959, 234:2145-2150
    • (1959) J Biol Chem , vol.234 , pp. 2145-2150
    • Jakoby, W.B.1    Fredericks, J.2
  • 18
    • 0022362907 scopus 로고
    • Control of utilization of L-arginine, L-ornithine, agmathine, and putrescine as nitrogen sources in Escherichia coli K-12
    • Snaibe E, Metzer E and Halpern YS Control of utilization of L-arginine, L-ornithine, agmathine, and putrescine as nitrogen sources in Escherichia coli K-12. J Bacteriol 1985, 163:938-942
    • (1985) J Bacteriol , vol.163 , pp. 938-942
    • Snaibe, E.1    Metzer, E.2    Halpern, Y.S.3
  • 20
    • 0027297771 scopus 로고
    • Aminotransferases: Demonstration of homology and division into evolutionary subgroups
    • Mehta PK, Hale TI and Christen P Aminotransferases: demonstration of homology and division into evolutionary subgroups. Eur J Biochem 1993, 214:549-561
    • (1993) Eur J Biochem , vol.214 , pp. 549-561
    • Mehta, P.K.1    Hale, T.I.2    Christen, P.3
  • 23
  • 26
    • 0016154301 scopus 로고
    • The 3′ terminal sequence of Escherichia coli 16S ribosomal RNA: Complementarity to nonsense triplets and ribosome binding sites
    • Shine J and Dalgarno L The 3′ terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites. Proc Natl Acad Sci USA 1974, 71:1342-1346
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 1342-1346
    • Shine, J.1    Dalgarno, L.2
  • 27
    • 0031827017 scopus 로고    scopus 로고
    • Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli
    • Shnaider BL, Kiupakis AK and Reitzer LJ Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli. J Bacteriol 1998, 180:4278-4286
    • (1998) J Bacteriol , vol.180 , pp. 4278-4286
    • Shnaider, B.L.1    Kiupakis, A.K.2    Reitzer, L.J.3
  • 28
    • 0029828233 scopus 로고    scopus 로고
    • Strategies for achieving high-level expression of genes in Escherichia coli
    • Makrides SC Strategies for achieving high-level expression of genes in Escherichia coli. Microbiol Rev 1996, 60:512-538
    • (1996) Microbiol Rev , vol.60 , pp. 512-538
    • Makrides, S.C.1
  • 29
    • 2642659608 scopus 로고
    • Translational efficiency of the Escherichia coli adenylate-cyclase gene - Mutating the UUG initiation codon to GUG or AUG resultes in increased gene-expression
    • Reddy P, Peterkofsky A and McKenney K Translational efficiency of the Escherichia coli adenylate-cyclase gene - mutating the UUG initiation codon to GUG or AUG resultes in increased gene-expression. Proc Natl Acad Sci USA 1985, 82:54656-5660
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 54656-55660
    • Reddy, P.1    Peterkofsky, A.2    McKenney, K.3
  • 32
    • 0017184389 scopus 로고
    • A rapid and sensitive method of for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM A rapid and sensitive method of for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976, 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 33
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature London 1970, 227:680-685
    • (1970) Nature London , vol.227 , pp. 680-685
    • Laemmli, U.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.