The Structure of Serotonin N-Acetyltransferase: Illustrating Catalysis by the GCN5-Related N-Acetyltransferase (GNAT) Enzyme Superfamily
نویسندگان
چکیده
منابع مشابه
Structure of the Histone Acetyltransferase Hat1 A Paradigm for the GCN5-Related N-acetyltransferase Superfamily
We have solved the crystal structure of the yeast histone acetyltransferase Hat1-acetyl coenzyme A (AcCoA) complex at 2.3 A resolution. Hat1 has an elongated, curved structure, and the AcCoA molecule is bound in a cleft on the concave surface of the protein, marking the active site of the enzyme. A channel of variable width and depth that runs across the protein is probably the binding site for...
متن کاملCrystal structure of the histone acetyltransferase Hpa2: A tetrameric member of the Gcn5-related N-acetyltransferase superfamily.
We report the crystal structure of the yeast protein Hpa2 in complex with acetyl coenzyme A (AcCoA) at 2.4 A resolution and without cofactor at 2.9 A resolution. Hpa2 is a member of the Gcn5-related N-acetyltransferase (GNAT) superfamily, a family of enzymes with diverse substrates including histones, other proteins, arylalkylamines and aminoglycosides. In vitro, Hpa2 is able to acetylate speci...
متن کاملCrystal Structure of a GCN5-Related N-acetyltransferase Serratia marcescens Aminoglycoside 3-N-acetyltransferase
The X-ray structure of a canonical GCN5-related N-acetyltransferase (GNAT), Serratia marcescens aminoglycoside 3-N-acetyltransferase, bound to coenzyme A (CoA) has been determined at 2.3 A resolution. The single domain alpha/beta protein resembles a cupped right hand wrapped around a cylinder and consists of a highly curved, six-stranded beta sheet of mixed polarity that is sandwiched between f...
متن کاملStructure and Functional Diversity of GCN5-Related N-Acetyltransferases (GNAT)
General control non-repressible 5 (GCN5)-related N-acetyltransferases (GNAT) catalyze the transfer of an acyl moiety from acyl coenzyme A (acyl-CoA) to a diverse group of substrates and are widely distributed in all domains of life. This review of the currently available data acquired on GNAT enzymes by a combination of structural, mutagenesis and kinetic methods summarizes the key similarities...
متن کاملAcetylation of serotonin in vitro by a human N-acetyltransferase.
1. There is a well-recognized genetic polymorphism for the N-acetylation of isoniazid and sulphamethazine by human livers. 2. Serotonin was found to be acetylated by human liver enzyme preparations and the N-acetylserotonin formed was identified and determined quantitatively. 3. In 13 livers examined there was a wide variability in the capacity to acetylate serotonin that did not correlate with...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Acta Crystallographica Section A Foundations of Crystallography
سال: 2000
ISSN: 0108-7673
DOI: 10.1107/s0108767300025514