Literature DB >> 1633194

Hydrogen bond network of cytochrome P-450cam: a network connecting the heme group with helix K.

K Yoshikawa1, T Noguti, M Tsujimura, H Koga, T Yasukochi, T Horiuchi, M Go.   

Abstract

During investigations of the structural character of a mutant P-450cam where Glu-286 is replaced with lysine, we obtained evidence of a hydrogen bond network between helix K and the heme group via helix L of P-450cam. This mutant protein loses the ability to maintain the heme group in a proper position, possibly due to a break in the hydrogen bond network.

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Year:  1992        PMID: 1633194     DOI: 10.1016/0167-4838(92)90124-v

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  1 in total

1.  The residue E351 is essential for the activity of human 21-hydroxylase: evidence from a naturally occurring novel point mutation compared with artificial mutants generated by single amino acid substitutions.

Authors:  Nils Krone; Felix G Riepe; Joachim Grötzinger; Carl-Joachim Partsch; Jürgen Brämswig; Wolfgang G Sippell
Journal:  J Mol Med (Berl)       Date:  2005-04-14       Impact factor: 4.599

  1 in total

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