DEAMINOFORMYCIN


Source	Gaulton A, Kale N, van Westen GJ, Bellis LJ, Bento AP, Davies M, Hersey A, Papadatos G, Forster M, Wege P, Overington JP. A large-scale crop protection bioassay data set. Sci Data. 2015 Jul 7;2:150032. Read more ...


Active Pharmaceutical Ingredients Bioactive chemicals	Exact Similarity SubStructure	Threshold (%) >= 70

Structure


InChI Key	OGBPXKPYHVPAOL-KBHCAIDQSA-N
Smiles	OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)c2n[nH]c3cncnc23
InChI	InChI=1S/C10H12N4O4/c15-2-5-8(16)9(17)10(18-5)7-6-4(13-14-7)1-11-3-12-6/h1,3,5,8-10,15-17H,2H2,(H,13,14)/t5-,8-,9-,10+/m1/s1

Physicochemical Descriptors

Property Name	Value
Molecular Formula	C10H12N4O4
Molecular Weight	252.23
AlogP	-1.44
Hydrogen Bond Acceptor	7.0
Hydrogen Bond Donor	4.0
Number of Rotational Bond	2.0
Polar Surface Area	124.38
Molecular species	NEUTRAL
Aromatic Rings	2.0
Heavy Atoms	18.0

Assay Description	Organism	Bioactivity
Binding affinity to Bos taurus (calf) intestinal mucosa adenylate deaminase	Bos taurus	35000.0 nM
Inhibition of Bos taurus (calf) intestinal mucosa adenylate deaminase	Bos taurus	5000.0 nM
Increase in ATP levels in Pisum sativum (pea) seedlings at 100 uM measured per gram of frozen weight after 24 hr by luciferase based assay (Rvb = 213 to 226 nmol/g of frozen weight)	Pisum sativum	693.0 nmol
Increase in ATP levels in Pisum sativum (pea) seedlings at 100 uM measured per gram of frozen weight after 4 hr by luciferase based assay (Rvb = 253 to 267 nmol/g of frozen weight)	Pisum sativum	423.0 nmol
Inhibition of adenylate deaminase	None	None

Cross References

Resources	Reference
ChEMBL	CHEMBL60235
PubChem	44302468
SureChEMBL	SCHEMBL5071997

CONTENTS


PREMIER has received funding from the Innovative Medicines Initiative 2 Joint Undertaking (JU) under grant agreement No 875508. The JU receives support from the EU’s Horizon 2020 research and innovation programme and the European Federation of Pharmaceutical Industries and Associations (EFPIA). The views reflect only the authors’ perspective and the JU is not responsible for any use that may be made of the information this manuscript contains. Elements of the website have been developed under projects PREMIER and the Biocenter Finland Drug Discovery and Chemical Biology network. CSC-IT is thanked for providing computational resources. Content of the website is provided without guarantee for correctness. Data has been collected and integrated from multiple public sources, for the largest: FDA, HUGO Gene Nomenclature Committee, ChEMBL, IUPHAR/BPS guide to pharmacology, Reactome, UniProt, and Ensembl. Credit is given to Ensembl for collecting species images (provided under public domain licences such as Wikimedia and NHGRI).

PREMIER has received funding from the Innovative Medicines Initiative 2 Joint Undertaking (JU) under grant agreement No 875508. The JU receives support from the EU’s Horizon 2020 research and innovation programme and the European Federation of Pharmaceutical Industries and Associations (EFPIA). The views reflect only the authors’ perspective and the JU is not responsible for any use that may be made of the information this manuscript contains.

Elements of the website have been developed under projects PREMIER and the Biocenter Finland Drug Discovery and Chemical Biology network. CSC-IT is thanked for providing computational resources. Content of the website is provided without guarantee for correctness. Data has been collected and integrated from multiple public sources, for the largest: FDA, HUGO Gene Nomenclature Committee, ChEMBL, IUPHAR/BPS guide to pharmacology, Reactome, UniProt, and Ensembl. Credit is given to Ensembl for collecting species images (provided under public domain licences such as Wikimedia and NHGRI).