2c75

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Image:2c75.gif

2c75, resolution 1.70Å

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FUNCTIONAL ROLE OF THE AROMATIC CAGE IN HUMAN MONOAMINE OXIDASE B: STRUCTURES AND CATALYTIC PROPERTIES OF TYR435 MUTANT PROTEINS

Overview

Current structural results of several flavin-dependent amine oxidizing, enzymes including human monoamine oxidases A and B (MAO A and MAO B) show, aromatic amino acid residues oriented approximately perpendicular to the, flavin ring, suggesting a functional role in catalysis. In the case of, human MAO B, two tyrosyl residues (Y398 and Y435) are found in the, substrate binding site on the re face of the covalent flavin ring [Binda, et al. (2002) J. Biol. Chem. 277, 23973-23976]. To probe the functional, significance of this structure, Tyr435 in MAO B was mutated with the amino, acids Phe, His, Leu, or Trp, the mutant proteins expressed in Pichia, pastoris, and purified to homogeneity. Each mutant protein contains, covalent FAD and exhibits a high level of catalytic functionality. No, major ... [(full description)]

About this Structure

2C75 is a [Single protein] structure of sequence from [Homo sapiens] with FAD as [ligand]. Active as [Amine oxidase (flavin-containing)], with EC number [1.4.3.4]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Functional role of the "aromatic cage" in human monoamine oxidase B: structures and catalytic properties of Tyr435 mutant proteins., Li M, Binda C, Mattevi A, Edmondson DE, Biochemistry. 2006 Apr 18;45(15):4775-84. PMID:16605246

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