OBSOLETE. Stops, prevents or reduces the activity of angiotensin-converting enzyme, thereby preventing the synthesis of angiotensin II from its precursor, angiotensin I.

The process of targeting specific proteins to the Golgi apparatus. Usually requires an organelle-specific protein sequence motif or a protein modification (for example a palmitoylation).

The reversible aggregation of misfolded proteins and chaperones, formed to shield thermosensitive proteins from degradation until conditions allow disaggregation and refolding.

OBSOLETE. Catalysis of the cleavage of 14-Ala-Leu-15 in insulin B chain and cleavage of 413-Lys-Leu-414 in alpha chain of fibrinogen.

Reversible aggregate of misfolded proteins and chaperones formed to shield thermosensitive proteins from degradation until conditions allow disaggregation and refolding.

OBSOLETE. Catalysis of the reaction: peptidylproline (omega=180) = peptidylproline (omega=0).

A secreted multiprotein complex composed of 4 proteins, regulating group size during aggregation in cooperative development. An example of this complex is found in Dictyostelium discoideum.

Removes a glycolipid from a membrane or a monolayer lipid particle, transports it through the aqueous phase while protected in a hydrophobic pocket, and brings it to an acceptor membrane or lipid particle. A glycolipid is a compound usually containing 1-4 linked monosaccharide residues joined by a glycosyl linkage to a lipid.

Removes a lipid from a membrane or a monolayer lipid particle, transports it through the aqueous phase while protected in a hydrophobic pocket, and brings it to an acceptor membrane or lipid particle. This results in intermembrane transfer of lipids.

OBSOLETE. 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.

A protein complex consisting of a regulatory subunit (alpha-MPP) and a catalytic subunit (beta-MPP) that catalyzes the release of N-terminal targeting peptides from precursor proteins imported into the mitochondrion.

A protein complex that catalyzes the reaction 3-methyl-2-oxobutanoate + lipoamide = S-(2-methylpropanoyl)-dihydrolipoamide + carbon dioxide (CO2). This requires thiamine diphosphate; the enzyme also acts on (S)-3-methyl-2-oxopentanoate and 4-methyl-2-oxo-pentanoate.

Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an insecticide stimulus. Insecticides are chemicals used to kill insects.

Catalysis of the reaction: 3'-phosphoadenosine 5'-phosphosulfate + heparan sulfate = adenosine 3',5'-bisphosphate + heparan sulfate 6-O-sulfate; results in 6-O-sulfation of glucosamine residues in heparan sulfate.

OBSOLETE. Catalysis of the cleavage of a Leu-Ser bond within the luminal loop of a sterol regulatory element binding protein (SREBP). This activity is the first of two sequential cleavage reactions and cleaves SREBP into two membrane-bound halves.

OBSOLETE. Catalysis of the hydrolysis of peptide bonds within a sterol regulatory element binding protein (SREBP). SREBPs are transcription factors that bind sterol regulatory elements (SREs), DNA motifs found in the promoters of target genes.

OBSOLETE. Catalysis of the cleavage, within the membrane-spanning helix, of the amino-terminal half (the intermediate form) of sterol regulatory element binding protein (SREBP). This activity releases the transcription factor domain of SREBP from the membrane, freeing it to enter the nucleus.