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Mammalian Nucleotidyl Cyclases and Their Nucleotide Binding Sites

Dove, Stefan (2016) Mammalian Nucleotidyl Cyclases and Their Nucleotide Binding Sites. In: Seifert, Roland, (ed.) Non-canonical Cyclic Nucleotides. Handbook of Experimental Pharmacology, 238. Springer International Publishing, Cham, Switzerland, pp. 49-66. ISBN 978-3-319-52673-7 (online), 978-3-319-52671-3 (print).

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Other URL: http://doi.org/10.1007/164_2015_34


Abstract

Mammalian membranous and soluble adenylyl cyclases (mAC, sAC) and soluble guanylyl cyclases (sGC) generate cAMP and cGMP from ATP and GTP, respectively, as substrates. mACs (nine human isoenzymes), sAC, and sGC differ in their overall structures owing to specific membrane-spanning and regulatory domains but consist of two similarly folded catalytic domains C1 and C2 with high structure-based ...

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Item type:Book section
Date:2016
Institutions:Chemistry and Pharmacy > Institute of Pharmacy > Pharmaceutical/Medicinal Chemistry II (Prof. Buschauer)
Identification Number:
ValueType
10.1007/164_2015_34DOI
Keywords:Binding modes, Inhibitors, Membranous adenylyl cyclase, Soluble adenylyl cyclase, Soluble guanylyl cyclase, Structure, Substrates
Dewey Decimal Classification:500 Science > 540 Chemistry & allied sciences
500 Science > 570 Life sciences
600 Technology > 610 Medical sciences Medicine
600 Technology > 615 Pharmacy
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Item ID:35776
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