The series of molecular signals within the cell that are mediated by a member of the Rac family of proteins switching to a GTP-bound active state.

A protein complex that contains flotillin-1 and flotillin-2, and may contain associated proteins. Flotillins associate into membrane microdomains resembling caveolae.

The action characteristic of growth hormone-releasing hormone, any of a family of peptide hormones that act on the anterior pituitary to stimulate the secretion of growth hormone and exert a trophic effect on the gland.

A nuclear body that is enriched in the lymphoid cell-specific protein LYSp100B; LANDs are globular, electron-dense structures and are morphologically distinct from the annular structures characteristic of PML bodies.

An enzyme complex containing a vanadium-iron cluster found in some species, such as Azotobacter vinelandii. It is composed of two proteins, dinitrogenase and nitrogenase reductase; dinitrogenase, the vanadium-iron protein, is tetrameric with an alpha2-beta2 structure, and nitrogenase reductase is a homodimer.

An enzyme complex composed of two proteins, dinitrogenase and nitrogenase reductase; dinitrogenase is tetrameric with an alpha2-beta2 structure and nitrogenase reductase is a homodimer, and both are associated with metal ions, which differ between species. Both proteins are required for the enzyme activity of the complex, the formation of oxidized ferredoxin and ammonia from reduced ferredoxin and nitrogen.

An enzyme complex containing a molybdenum-iron cluster found in many species. It is composed of two proteins, dinitrogenase and nitrogenase reductase; dinitrogenase, the molybdenum-iron protein, is tetrameric with an alpha2-beta2 structure, and nitrogenase reductase is a homodimer.

An enzyme complex containing an iron-iron cluster found in species such as the photosynthetic bacterium Rhodobacter capsulatus. It is composed of two main subunits, dinitrogenase and nitrogenase reductase. Dinitrogenase, the iron-iron containing subunit, has an alpha1-beta2 or alpha2-beta2 structure, and the nitrogenase reductase subunit is a homodimer. Functions in the catalysis of the formation of oxidized ferredoxin and ammonia from reduced ferredoxin and nitrogen.

Catalysis of the reaction: D-glycerate + NADP+ = hydroxypyruvate + NADPH + H+.

Catalysis of the reaction: 4-hydroxy-L-proline + NAD+ = 4-oxoproline + NADH + H+.

OBSOLETE. Catalysis of an oxidation-reduction (redox) reaction in which an aldehyde or ketone (oxo) group acts as a hydrogen or electron donor and reduces an acceptor other than NAD, NADP, oxygen, an iron-sulfur protein, disulphide or a cytochrome.

Catalysis of an oxidation-reduction (redox) reaction in which an aldehyde or ketone (oxo) group acts as a hydrogen or electron donor and reduces a cytochrome.

Catalysis of the reaction: cinnamaldehyde + CoA + NADP+ = cinnamoyl-CoA + NADPH + H+.

Catalysis of the reaction: 8-[(1R,2R)-3-oxo-2-{(Z)-pent-2-en-1-yl}cyclopentyl]octanoate + NADP(+) = (15Z)-12-oxophyto-10,15-dienoate + H(+) + NADPH.

OBSOLETE. Catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces an acceptor other than quinone or related compound, a cytochrome, an iron-sulfur protein, NAD, NADP or oxygen.

Catalysis of the reaction: L-galactono-1,4-lactone + 2 ferricytochrome c = L-ascorbate + 2 ferrocytochrome c.

Catalysis of the reaction: acyl-[acyl-carrier protein] + NAD(P)+ = trans-2,3-dehydroacyl-[acyl-carrier protein] + NAD(P)H + H+.

Catalysis of the reaction: chlorophyllide a + NADP+ = protochlorophyllide + NADPH + H+.