Literature summary for 1.19.1.1 extracted from

Bortolotti, A.; Perez-Dorado, I.; Goni, G.; Medina, M.; Hermoso, J.A.; Carrillo, N.; Cortez, N.
Coenzyme binding and hydride transfer in Rhodobacter capsulatus ferredoxin/flavodoxin NADP(H) oxidoreductase (2009), Biochim. Biophys. Acta, 1794, 199-210.

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Rhodobacter capsulatus

Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with 2'-phospho-AMP and NADP+. In the complexes obtained, the nucleotides bind exclusively through the adenosine moiety. The adenosine moiety binds into a cavity formed by residues of conserved segments, i.e residues 128 to 130, residues 158 to 163, residues 193 to 205, and residues 233 to 240. The adenosine binding site is essentially formed by residues R158, R195 and R203, which stabilise the nucleotide	Rhodobacter capsulatus

Crystallization (Comment)

Organism

in complex with 2'-phospho-AMP and NADP+. In the complexes obtained, the nucleotides bind exclusively through the adenosine moiety. The adenosine moiety binds into a cavity formed by residues of conserved segments, i.e residues 128 to 130, residues 158 to 163, residues 193 to 205, and residues 233 to 240. The adenosine binding site is essentially formed by residues R158, R195 and R203, which stabilise the nucleotide

Rhodobacter capsulatus

Organism

Organism	UniProt	Comment	Textmining
Rhodobacter capsulatus	Q9L6V3	enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1	-

Cofactor

Cofactor	Comment	Organism	Structure
NADP+	Kd value 0.222 mM, coenzyme docking occurrs through the 2'-P-AMP moiety	Rhodobacter capsulatus

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Release 2023.1 (January 2023)