X-ray diffraction study of Penicillium Vitale catalase in the complex with aminotriazole

Journal Article · Fri Jul 15 00:00:00 EDT 2011 · Crystallography Reports

DOI:https://doi.org/10.1134/S1063774511030060· OSTI ID:22054276

Borovik, A A; Grebenko, A I

The three-dimensional structure of the enzyme catalase from Penicillium vitale in a complex with the inhibitor aminotriazole was solved and refined by protein X-ray crystallography methods. An analysis of the three-dimensional structure of the complex showed that the inhibition of the enzyme occurs as a result of the covalent binding of aminotriazole to the amino-acid residue His64 in the active site of the enzyme. An investigation of the three-dimensional structure of the complex resulted in the amino-acid residues being more precisely identified. The binding sites of saccharide residues and calcium ions in the protein molecule were found.

• OSTI ID: 22054276
• Journal Information: Crystallography Reports, Vol. 56, Issue 4; Other Information: Copyright (c) 2011 Pleiades Publishing, Ltd.; Country of input: International Atomic Energy Agency (IAEA); ISSN 1063-7745
• Country of Publication: United States
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
AMINO ACIDS
CALCIUM IONS
CATALASE
CHEMICAL BONDS
CRYSTALLOGRAPHY
ENZYME INHIBITORS
PENICILLIUM
TRIAZOLES
X-RAY DIFFRACTION