Literature summary for 2.5.1.75 extracted from

Chu, H.M.; Ko, T.P.; Wang, A.H.
Crystal structure and substrate specificity of plant adenylate isopentenyltransferase from Humulus lupulus: distinctive binding affinity for purine and pyrimidine nucleotides (2010), Nucleic Acids Res., 38, 1738-1748.

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Cloned(Commentary)

Cloned (Comment)	Organism
overexpressed as a N-terminal hexahistidine tag protein in Escherichia coli BL21 (DE3)	Humulus lupulus

Crystallization (Commentary)

Crystallization (Comment)	Organism
The crystal structure of the AIPT-ATP complex from Humulus lupulus is similar to the previous structures of Agrobacterium AIPT and yeast tRNA-IPT. The enzyme is structurally homologous to the NTP-binding kinase family of proteins but forms a solvent-accessible channel that binds to the donor substrate dimethylallyl diphosphate, which is directed toward the acceptor substrate ATP/ADP.	Humulus lupulus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
dimethylallyl diphosphate + adenine37 in tRNA	Humulus lupulus	-	diphosphate + N6-dimethylallyladenine37 in tRNA	-	ir

Organism

Organism	UniProt	Comment	Textmining
Humulus lupulus	Q5GHF7	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
dimethylallyl diphosphate + adenine37 in tRNA	-	Humulus lupulus	diphosphate + N6-dimethylallyladenine37 in tRNA	-	ir

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Release 2023.1 (January 2023)