Title of article :
Conversion of a Guanylyl Cyclase to an Adenylyl Cyclase
Author/Authors :
Beuve، Annie نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 1999
Pages :
-544
From page :
545
To page :
0
Abstract :
Guanylyl cyclases catalyze the formation of cGMP from GTP, but display extensive identity at the catalytic domain primary amino acid level with the adenylyl cyclases. The recent solving of the crystal structures of soluble forms of adenylyl cyclase has resulted in predictions of those amino acids important for substrate specificity. Modeling of a membrane-bound homodimeric guanylyl cyclase predicted the comparable amino acids that would interact with the guanine ring. Based on these structural data, the replacement of three key residues in the heterodimeric form of soluble guanylyl cyclase has led to a complete conversion in substrate specificity. Furthermore, the mutant enzyme remained fully sensitive to sodium nitroprusside, a nitric oxide donor.
Keywords :
interleukin-18 , interferon GAMMA , cytokines
Journal title :
METHODS : A COMPANION TO METHODS IN ENZYMOLOGY
Serial Year :
1999
Journal title :
METHODS : A COMPANION TO METHODS IN ENZYMOLOGY
Record number :
58135
Link To Document :
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