Structure ofMesorhizobium lotiarylamineN-acetyltransferase 1
نویسندگان
چکیده
منابع مشابه
Structure of Mesorhizobium loti arylamine N-acetyltransferase 1.
The arylamine N-acetyltransferase (NAT) enzymes have been found in a broad range of both eukaryotic and prokaryotic organisms. The NAT enzymes catalyse the transfer of an acetyl group from acetyl Co-enzyme A onto the terminal nitrogen of a range of arylamine, hydrazine and arylhydrazine compounds. Recently, several NAT structures have been reported from different prokaryotic sources including S...
متن کاملNAT 1 ( N - acetyltransferase 1 ( arylamine N - acetyltransferase ) )
The human NAT1 gene has nine exons. The coding region is located in exon 9 and spans 870 bp. Diverse NAT1 transcripts have been reported and two promoters exist. The first promoter, designated as P1 is located in the 5' flanking region of exon 1 and controls two major (a1 and a2) transcripts. The second promoter is located upstream of exon 4 and give rise to at least five (b1 to b5) different t...
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MOF was first identified in Drosophila melanogaster as an important component of the dosage compensation complex. As a member of MYST family of histone acetyltransferase, MOF specifically deposits the acetyl groups to histone H4 lysine 16. Throughout evolution, MOF and its mammalian ortholog have retained highly conserved substrate specificity and similar enzymatic activities. MOF plays importa...
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The results of modeling of a novel human histone acetyltransferase Patt1 are presented here. This protein belongs to the GNAT GCN5 family and shows proapoptotic activity in human hepatocellular carcinoma cells. Patt1 is an attractive therapeutic target. The sequence analysis, fold recognition predictions and homology modeling of Patt1 protein structure were performed. N- and C- termini of Patt1...
متن کاملStructure 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...
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ژورنال
عنوان ژورنال: Acta Crystallographica Section F Structural Biology and Crystallization Communications
سال: 2004
ISSN: 1744-3091
DOI: 10.1107/s1744309104030659