Site-Directed Mutagenesis Studies on a Putative Fifth Iron Ligand of Mouse 8S-Lipoxygenase: Retention of Catalytic Activity on Mutation of Serine-558 to Asparagine, Histidine, or Alanine-Reference-Cited by-同舟云学术

Site-Directed Mutagenesis Studies on a Putative Fifth Iron Ligand of Mouse 8S-Lipoxygenase: Retention of Catalytic Activity on Mutation of Serine-558 to Asparagine, Histidine, or Alanine

Published:2001-02 Issue:2 Volume:386 Page:136-142
ISSN:0003-9861
Container-title:Archives of Biochemistry and Biophysics
language:en
Short-container-title:Archives of Biochemistry and Biophysics

Author:

Jisaka Mitsuo,Boeglin William E.,Kim Richard B.,Brash Alan R.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference43 articles.

1. Lipoxygenases: Occurrence, Functions, Catalysis, and Acquisition of Substrate

2. The Three-Dimensional Structure of an Arachidonic Acid 15-Lipoxygenase

3. Crystallographic determination of the active site iron and its ligands in soybean lipoxygenase L-1

4. Crystal Structure of Soybean Lipoxygenase L-1 at 1.4 Å Resolution,

5. Structure of soybean lipoxygenase L3 and a comparison with its L1 isoenzyme

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