Disturbances on Delta aminolevulinate dehydratase (ALA-D) enzyme activity by Pb2+, Cd2+, Cu2+, Mg2+, Zn2+, Na+, K+ and Li+: analysis based on coordination geometry and acid–base Lewis capacity-Reference-Cited by-同舟云学术

Disturbances on Delta aminolevulinate dehydratase (ALA-D) enzyme activity by Pb2+, Cd2+, Cu2+, Mg2+, Zn2+, Na+, K+ and Li+: analysis based on coordination geometry and acid–base Lewis capacity

Published:2005-02 Issue:2 Volume:99 Page:409-414
ISSN:0162-0134
Container-title:Journal of Inorganic Biochemistry
language:en
Short-container-title:Journal of Inorganic Biochemistry

Author:

Pauza N.L.,Cotti M.J. Pérez,Godar L.,de Sancovich A.M. Ferramola,Sancovich H.A.

Publisher

Elsevier BV

Subject

Inorganic Chemistry,Biochemistry

Reference44 articles.

1. The Quaternary Structure of -Aminolevulinic Acid Dehydratase from Bovine Liver

2. Influencing its molecular weight determination

3. Characterization of the two 5-aminolaevulinic acid binding sites, the A- and P-sites, of 5-aminolaevulinic acid dehydratase from Escherichia coli

4. The Enzymes;Shemin,1972

5. 5-Chlorolevulinate modification of porphobilinogen synthase identifies a potential role for the catalytic zinc

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