메뉴 건너뛰기




Volumn 168, Issue 6, 1997, Pages 457-463

3-Methylaspartate ammonia-lyase as a marker enzyme of the mesaconate pathway for (S)-glutamate fermentation in Enterobacteriaceae

Author keywords

(S) Citramalate hydrolase; (S) Glutamate fermentation; 3 Methylaspartase; Enterobacteriaceae, Citrobacter; Glutamate mutase; Morganella

Indexed keywords

GLUTAMIC ACID; LYASE; MUTASE;

EID: 0030729079     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002030050522     Document Type: Article
Times cited : (35)

References (17)
  • 1
    • 37049086056 scopus 로고
    • Kinetics and mechanism of synelimination of ammonia from (2S,3R)-3-methylaspartic acid by β-methylaspartase
    • Archer CH, Gani D (1993) Kinetics and mechanism of synelimination of ammonia from (2S,3R)-3-methylaspartic acid by β-methylaspartase. J Chem Soc Chem Commun, pp 140-142
    • (1993) J Chem Soc Chem Commun , pp. 140-142
    • Archer, C.H.1    Gani, D.2
  • 2
    • 85007940552 scopus 로고
    • Occurrence of 3-methylaspartate ammonia-lyase in facultative anaerobes and their application to synthesis of 3-substituted (S)-aspartic acids
    • Asano Y, Kato Y (1994a) Occurrence of 3-methylaspartate ammonia-lyase in facultative anaerobes and their application to synthesis of 3-substituted (S)-aspartic acids. Biosci Biotechnol Biochem 58:223-224
    • (1994) Biosci Biotechnol Biochem , vol.58 , pp. 223-224
    • Asano, Y.1    Kato, Y.2
  • 3
    • 0028334273 scopus 로고
    • Crystalline 3-methylaspartase from a facultative anaerobe, Escherichia coli strain YG-1002
    • Asano Y, Kato Y (1994b) Crystalline 3-methylaspartase from a facultative anaerobe, Escherichia coli strain YG-1002. FEMS Microbiol Lett 118:255-258
    • (1994) FEMS Microbiol Lett , vol.118 , pp. 255-258
    • Asano, Y.1    Kato, Y.2
  • 5
    • 0014026991 scopus 로고
    • Assay and purification of (+)-citramalate hydro-lyase components from Clostridium tetanomorphum
    • Blair AH, Barker HA (1966) Assay and purification of (+)-citramalate hydro-lyase components from Clostridium tetanomorphum. J Biol Chem 241:400-408
    • (1966) J Biol Chem , vol.241 , pp. 400-408
    • Blair, A.H.1    Barker, H.A.2
  • 6
    • 0024291639 scopus 로고
    • Primary deuterium isotope effects for the 3-methylaspartase-catalyzed deamination of (2S)-aspartic acid, (2S,3S)-3-methylaspartic acid, and (2S,3S)-3-ethylaspartic acid
    • Botting NP, Cohen MA, Akhtar M, Gani D (1988) Primary deuterium isotope effects for the 3-methylaspartase-catalyzed deamination of (2S)-aspartic acid, (2S,3S)-3-methylaspartic acid, and (2S,3S)-3-ethylaspartic acid. Biochemistry 27:2956-2959
    • (1988) Biochemistry , vol.27 , pp. 2956-2959
    • Botting, N.P.1    Cohen, M.A.2    Akhtar, M.3    Gani, D.4
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the 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
  • 8
    • 0015994398 scopus 로고
    • Two pathways of glutamate fermentation by anaerobic bacteria
    • Buckel W, Barker HA (1974) Two pathways of glutamate fermentation by anaerobic bacteria. J Bacteriol 117:1248-1260
    • (1974) J Bacteriol , vol.117 , pp. 1248-1260
    • Buckel, W.1    Barker, H.A.2
  • 9
    • 0027266842 scopus 로고
    • Oxic and anoxic growth of a new Citrobacter species on amino acids
    • Gerritse J, Gottschal JC (1993) Oxic and anoxic growth of a new Citrobacter species on amino acids. Arch Microbiol 160: 51-61
    • (1993) Arch Microbiol , vol.160 , pp. 51-61
    • Gerritse, J.1    Gottschal, J.C.2
  • 10
    • 0026469359 scopus 로고
    • Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding β-methylaspartase and characterization of the recombinant protein
    • Goda SK, Minton NP, Botting NP, Gani D (1992) Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding β-methylaspartase and characterization of the recombinant protein. Biochemistry 31:10747-10756
    • (1992) Biochemistry , vol.31 , pp. 10747-10756
    • Goda, S.K.1    Minton, N.P.2    Botting, N.P.3    Gani, D.4
  • 11
    • 77956939611 scopus 로고
    • The enzymic elimination of ammonia
    • Boyer PD (ed) Academic Press, New York
    • Hanson K, Havir EA (1972) The enzymic elimination of ammonia. In: Boyer PD (ed) The enzymes, 3rd edn, vol 7. Academic Press, New York, pp 75-164
    • (1972) The Enzymes, 3rd Edn , vol.7 , pp. 75-164
    • Hanson, K.1    Havir, E.A.2
  • 12
    • 85007810217 scopus 로고
    • Purification and properties of crystalline 3-Methylaspartase from two facultative anaerobes, Citrobacter sp. strain YG- 0504 and Morganella morganii strain YG-0601
    • Kato Y, Asano Y (1995a) Purification and properties of crystalline 3-Methylaspartase from two facultative anaerobes, Citrobacter sp. strain YG-0504 and Morganella morganii strain YG-0601. Biosci Biotechnol Biochem 59:93-99
    • (1995) Biosci Biotechnol Biochem , vol.59 , pp. 93-99
    • Kato, Y.1    Asano, Y.2
  • 13
    • 0028973507 scopus 로고
    • 3-Methylaspartate ammonia-lyase from a facultative anaerobe strain YG-1002
    • Kato Y, Asano Y (1995b) 3-Methylaspartate ammonia-lyase from a facultative anaerobe strain YG-1002. Appl Microbiol Biotechnol 43:901-907
    • (1995) Appl Microbiol Biotechnol , vol.43 , pp. 901-907
    • Kato, Y.1    Asano, Y.2
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0015292219 scopus 로고
    • Alternate pathway for isoleucine biosynthesis in Escherichia coli
    • Phillips AT, Nuss JI, Moosic J, Foshay C (1972) Alternate pathway for isoleucine biosynthesis in Escherichia coli. J Bacteriol 109:714-719
    • (1972) J Bacteriol , vol.109 , pp. 714-719
    • Phillips, A.T.1    Nuss, J.I.2    Moosic, J.3    Foshay, C.4
  • 17
    • 0026353977 scopus 로고
    • Reduction of N-oxides and sulfoxide by the same terminal reductase in Proteus mirabilis
    • Valentine-Serano A, Hudspeth MES, Meganathan R (1991) Reduction of N-oxides and sulfoxide by the same terminal reductase in Proteus mirabilis. Curr Microbiol 23:271-276
    • (1991) Curr Microbiol , vol.23 , pp. 271-276
    • Valentine-Serano, A.1    Hudspeth, M.E.S.2    Meganathan, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.