About: Structure of the ForT/PRPP complex uncovers the mechanism of C-C bond formation in C-nucleotide antibiotic biosynthesis

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About: Structure of the ForT/PRPP complex uncovers the mechanism of C-C bond formation in C-nucleotide antibiotic biosynthesis Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Structure of the ForT/PRPP complex uncovers the mechanism of C-C bond formation in C-nucleotide antibiotic biosynthesis
Creator	Zhu, Wen Li, W Liu, H Zhu, W Gao, S Li, Wenbo De Crécy-Lagard, Valérie Gao [+], ] Gao, Sisi Liu, Huanting Naismith, J Naismith, James Radadiya [+], Radadiya, Ashish Richards, N Richards, Nigel
Source	BioRxiv
abstract	C-C bond formation is at the heart of anabolism and organic chemistry, but relatively few enzymatic strategies for catalyzing this reaction are known. The enzyme ForT catalyzes C-C bond formation between 5’-phosphoribosyl-1’-pyrophosphate (PRPP) and 4-amino-1H-pyrazole-3,5-dicarboxylate to make a key intermediate in the biosynthesis of the C-nucleotide formycin A 5’-phosphate; we now report the 2.5 Å resolution structure of the ForT/PRPP complex and thus locate the active site. Site-directed mutagenesis has identified those residues critical for PRPP recognition and catalysis. Structural conservation with GHMP kinases suggests that stabilization of the negatively charged pyrophosphate leaving group is crucial for catalysis in ForT. A mechanism for this new class of C-C bond forming enzymes is proposed. Entry for the Table of Contents A new class of enzymes catalyse C-C bond formation by irreversible CO2 and pyrophosphate production.
has issue date	2020-03-30(xsd:dateTime)
bibo:doi	10.1101/2020.03.26.009662
has license	biorxiv
sha1sum (hex)	3908bbcef5a528abbc3749c2b7faa63ba5c8bb05
schema:url	https://doi.org/10.1101/2020.03.26.009662
resource representing a document's title	Structure of the ForT/PRPP complex uncovers the mechanism of C-C bond formation in C-nucleotide antibiotic biosynthesis
schema:publication	bioRxiv
resource representing a document's body	covid:3908bbcef5a528abbc3749c2b7faa63ba5c8bb05#body_text
is schema:about of	named entity 'resolution' named entity 'catalyzes' named entity 'enzymes' named entity 'strategies' named entity 'biosynthesis' named entity 'pyrophosphate' named entity 'biosynthesis' named entity 'Structure' named entity 'antibiotic' named entity 'STRATEGIES' named entity 'BIOSYNTHESIS' named entity 'FORT' named entity 'ENZYMES' covid:arg/3908bbcef5a528abbc3749c2b7faa63ba5c8bb05 named entity 'mechanism' named entity 'intermediate' named entity 'catalyzing' named entity 'phosphate' named entity 'amino' named entity 'anabolism' named entity 'complex' named entity 'negatively charged' named entity 'kinases' named entity 'anabolism' named entity 'pyrazole' named entity 'pyrophosphate' named entity 'PRPP' named entity 'PRPP' named entity 'pyrophosphate' named entity 'biosynthesis' named entity 'C-C bond' named entity 'pyrophosphate' named entity 'phosphate' named entity 'ADP' named entity 'substrates' named entity 'salt bridge' named entity 'molecule' named entity 'dimer' named entity 'conformationally' named entity 'aromatic' named entity 'salt bridges' named entity 'aromatic' named entity 'nucleoside' named entity 'nucleophilic attack' named entity 'helical' named entity 'ITC' named entity 'PRPP' named entity 'pyrophosphate' named entity 'ion' named entity 'reaction product' named entity 'kinases' named entity 'moiety' named entity 'b-sheets' named entity 'homoserine kinase' named entity 'mevalonate kinase' named entity 'dissociation constant' named entity 'phosphate' named entity 'kinase' named entity 'Gel filtration' named entity 'mevalonate kinase' named entity 'substrate' named entity 'phosphate' named entity 'homoserine kinase' named entity 'CO2' named entity 'multi-angle light scattering' named entity 'PDB' named entity 'pyrophosphate' named entity 'methanopterin' named entity 'biosynthetic'

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