Literature DB >> 6361021

Appendix. Purification, molecular weight, and NH2-terminal sequence of cystathionine gamma-synthase of Escherichia coli.

S V Tran, E Schaeffer, O Bertrand, R Mariuzza, P Ferrara.   

Abstract

The cystathionine gamma-synthase of Escherichia coli has been purified to homogeneity. It is a tetramer (Mr = 160,000) composed of identical subunits (Mr approximately 40,000). We have determined its amino acid terminal sequence and thus localized the starting codon of the metB structural gene.

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Year:  1983        PMID： 6361021

Source DB:  PubMed          Journal:  J Biol Chem        ISSN： 0021-9258            Impact factor:   5.157


  3 in total

1.  Crystal structure of Escherichia coli cystathionine gamma-synthase at 1.5 A resolution.

Authors:  T Clausen; R Huber; L Prade; M C Wahl; A Messerschmidt
Journal:  EMBO J       Date:  1998-12-01       Impact factor: 11.598

2.  The hyperthermophilic cystathionine γ-synthase from the aerobic crenarchaeon Sulfolobus tokodaii: expression, purification, crystallization and structural insights.

Authors:  Dan Sato; Tomoo Shiba; Sae Mizuno; Ayaka Kawamura; Shoko Hanada; Tetsuya Yamada; Mai Shinozaki; Masahiko Yanagitani; Takashi Tamura; Kenji Inagaki; Shigeharu Harada
Journal:  Acta Crystallogr F Struct Biol Commun       Date:  2017-02-21       Impact factor: 1.056

3.  Nucleotide sequence and biochemical characterization of the metJ gene from Salmonella typhimurium LT2.

Authors:  M L Urbanowski; G V Stauffer
Journal:  Nucleic Acids Res       Date:  1985-02-11       Impact factor: 16.971
  3 in total

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