This enzyme complex catalyzes the release of N-terminal targeting peptides from precursor proteins imported into the mitochondrion.

Catalysis of the hydrolysis of the terminal bond of Xaa-Pro-Xaa motifs to release unblocked, N-terminal dipeptides from substrates including Ala-Pro-para-nitroanilide and (sequentially, at the second, fourth and sixth bonds) of the motif Tyr-Pro-Phe-Pro-Gly-Pro-Ile.

Enables the directed movement of glycolipids, compounds containing (usually) 1-4 linked monosaccharide residues joined by a glycosyl linkage to a lipid, into, out of, within or between cells.

The chemical reactions involving fructose, the ketohexose arabino-2-hexulose. Fructose exists in a open chain form or as a ring compound. D-fructose is the sweetest of the sugars and is found free in a large number of fruits and honey.

The chemical reactions involving fructose 6-phosphate, also known as F6P. The D-enantiomer is an important intermediate in glycolysis, gluconeogenesis, and fructose metabolism.

The chemical reactions involving fructose 2,6-bisphosphate. The D enantiomer is an important regulator of the glycolytic and gluconeogenic pathways. It inhibits fructose 1,6-bisphosphatase and activates phosphofructokinase.

The chemical reactions involving fucose, or 6-deoxygalactose, which has two enantiomers, D-fucose and L-fucose.

The formation from simpler components of L-fucose (6-deoxy-L-galactose).

The chemical reactions involving glucose, the aldohexose gluco-hexose. D-glucose is dextrorotatory and is sometimes known as dextrose; it is an important source of energy for living organisms and is found free as well as combined in homo- and hetero-oligosaccharides and polysaccharides.

Interacting selectively with the U6 small nuclear RNA (U6 snRNA).

The breakdown into simpler components of glucose, the aldohexose gluco-hexose.

intracellular cyclic nucleotide activated cation channel complex

Catalysis of the cleavage of the N-propeptide of collagen chain alpha-1(I) at Pro-Gln and of alpha-1(II) and alpha-2(I) chains at Ala-Gln.