Anthrax lethal factor endopeptidase
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.24 Metalloendopeptidases > 3.4.24.83 anthrax lethal factor endopeptidase
Ste24 endopeptidase is an integral membrane zinc metalloendopeptidase, the type example of peptidase family M48, that hydrolyzes proteins terminating in a CaaX motif, where C is an S-isoprenylated cysteine, a is usually aliphatic and X is the C-terminal residue. It is one of two enzymes processing mating a-factor in yeast; after cleavage the S-isoprenylated cysteine at the new C-terminus is methyl-esterified to form a membrane anchor. It differs from intramembrane prenyl-peptidase Rce1 (EC 3.4.26.1). It hydrolyzes -P2-(S-farnesyl or geranylgeranyl)C-P1'-P2'-P3'-COOH, where P1' and P2' carry aliphatic side chains. In membranes it trims prenylated proteins. It features an M48-family zinc catalytic site embedded in the membrane.
Ste24 endopeptidase is an integral membrane zinc metalloendopeptidase, the type example of peptidase family M48, that hydrolyzes proteins terminating in a CaaX motif, where C is an S-isoprenylated cysteine, a is usually aliphatic and X is the C-terminal residue. It is one of two enzymes processing mating a-factor in yeast; after cleavage the S-isoprenylated cysteine at the new C-terminus is methyl-esterified to form a membrane anchor. It differs from intramembrane prenyl-peptidase Rce1 (EC 3.4.26.1). It hydrolyzes -P2-(S-farnesyl or geranylgeranyl)C-P1'-P2'-P3'-COOH, where P1' and P2' carry aliphatic side chains. In membranes it trims prenylated proteins. It features an M48-family zinc catalytic site embedded in the membrane.
References:
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