Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes

• Published in: Structure (London) Vol. 4; no. 3; pp. 287 - 298
• Main Authors: Conti, Elena, Franks, Nick P, Brick, Peter
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 15.03.1996
• Subjects: acyl-coenzyme A ligase; Adenosine - metabolism; adenylate; Amino Acid Sequence; Animals; Binding Sites; Coenzyme A Ligases - metabolism; Coleoptera - chemistry; Coleoptera - enzymology; Crystallization; Crystallography, X-Ray; firefly luciferase; Luciferases - chemistry; Molecular Sequence Data; Molecular Structure; Peptide Synthases - metabolism; peptide synthetase; Protein Structure, Secondary; Stereoisomerism; X-ray crystallography; X-ray crystallography; peptide synthetase; adenylate; firefly luciferase; acyl-coenzyme A ligase

Background: Firefly luciferase is a 62 kDa protein that catalyzes the production of light. In the presence of MgATP and molecular oxygen, the enzyme oxidizes its substrate, firefly luciferin, emitting yellow-green light. The reaction proceeds through activation of the substrate to form an adenylate...