Literature DB >> 4817962

The mechanism of action of ethanolamine ammonia-lyase, a B12-dependent enzyme. Evidence for two intermediates in the catalytic process.

T J Carty, B M Babior, R H Abeles.   

Abstract

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Year:  1974        PMID： 4817962

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


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  3 in total

1.  Expression, crystallization and preliminary X-ray crystallographic study of ethanolamine ammonia-lyase from Escherichia coli.

Authors:  Naoki Shibata; Hiroko Tamagaki; Shungo Ohtsuki; Naoki Hieda; Keita Akita; Hirofumi Komori; Yasuhito Shomura; Shin-ichi Terawaki; Tetsuo Toraya; Noritake Yasuoka; Yoshiki Higuchi
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2010-05-29

2.  Reaction of the Co(II)-substrate radical pair catalytic intermediate in coenzyme B12-dependent ethanolamine ammonia-lyase in frozen aqueous solution from 190 to 217 K.

Authors:  Chen Zhu; Kurt Warncke
Journal:  Biophys J       Date:  2008-09-19       Impact factor: 4.033

3.  The mechanism of cobalamin-dependent rearrangements.

Authors:  J S Krouwer; B M Babior
Journal:  Mol Cell Biochem       Date:  1977-04-12       Impact factor: 3.396
  3 in total

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