Biomaterial Database

Modification of arginyl residues in ferredoxin-NADP+ reductase from spinach leaves. 1979

G Zanetti, and C Gozzer, and G Sacchi, and B Curti

Reaction of spinach leaves ferredoxin-NADP+ reductase (NADPH:ferredoxin oxidoreductase, EC 1.6.7.1) with alpha-dicarbonyl compounds results in a biphasic loss of activity. The rapid phase yields modified enzyme with about 30% of the original activity, but no change in the Km for NADPH. Only partial protection against inactivation is provided by NADP+, NADPH and their analogs, whereas ferredoxin affords complete protection. The reductase inactivated to 30% of original activity shows a loss of about two arginyl residues, whereas only one residue is lost in the NADP+-protected enzymes. The data suggest that the integrity of at least two arginyl residues are requested for maximal activity of ferredoxin-NADP+ reductase: one residue being located near the NADP+-binding site, the other presumably situated in the ferredoxin-binding domain.

UI	MeSH Term	Description	Entries
D007700	Kinetics	The rate dynamics in chemical or physical systems.
D008024	Ligands	A molecule that binds to another molecule, used especially to refer to a small molecule that binds specifically to a larger molecule, e.g., an antigen binding to an antibody, a hormone or neurotransmitter binding to a receptor, or a substrate or allosteric effector binding to an enzyme. Ligands are also molecules that donate or accept a pair of electrons to form a coordinate covalent bond with the central metal atom of a coordination complex. (From Dorland, 27th ed)	Ligand
D009247	NADH, NADPH Oxidoreductases	A group of oxidoreductases that act on NADH or NADPH. In general, enzymes using NADH or NADPH to reduce a substrate are classified according to the reverse reaction, in which NAD+ or NADP+ is formally regarded as an acceptor. This subclass includes only those enzymes in which some other redox carrier is the acceptor. (Enzyme Nomenclature, 1992, p100) EC 1.6.	Oxidoreductases, NADH, NADPH,NADPH Oxidoreductases NADH,Oxidoreductases NADH, NADPH
D010944	Plants	Multicellular, eukaryotic life forms of kingdom Plantae. Plants acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations. It is a non-taxonomical term most often referring to LAND PLANTS. In broad sense it includes RHODOPHYTA and GLAUCOPHYTA along with VIRIDIPLANTAE.	Plant
D002074	Butanones	Derivatives of butanone, also known as methyl ethyl ketone (with structural formula CH3COC2H5).
D003510	Cyclohexanes	Six-carbon alicyclic hydrocarbons.
D003512	Cyclohexanones	Cyclohexane ring substituted by one or more ketones in any position.
D003931	Diacetyl	Carrier of aroma of butter, vinegar, coffee, and other foods.	2,3-Butanedione,Biacetyl,Diketobutane,Dimethyldiketone,Dimethylglyoxal,2,3 Butanedione
D005287	Ferredoxin-NADP Reductase	An enzyme that catalyzes the oxidation and reduction of FERREDOXIN or ADRENODOXIN in the presence of NADP. EC 1.18.1.2 was formerly listed as EC 1.6.7.1 and EC 1.6.99.4.	Adrenodoxin Reductase,Iron-Sulfur Protein Reductase,NADPH-Ferredoxin Reductase,Ferredoxin NADP Reductase,Iron Sulfur Protein Reductase,NADPH Ferredoxin Reductase,Protein Reductase, Iron-Sulfur,Reductase, Adrenodoxin,Reductase, Ferredoxin-NADP,Reductase, Iron-Sulfur Protein,Reductase, NADPH-Ferredoxin
D006037	Glyoxal	A 2-carbon aldehyde with carbonyl groups on both carbons.	Ethanedial,Ethanedione