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Proteins/UNIPROT:P28838
Cytosolic metallopeptidase that catalyzes the removal of unsubstituted N-terminal hydrophobic amino acids from various peptides. The presence of Zn(2+) ions is essential for the peptidase activity, and the association with other cofactors can modulate the substrate spectificity of the enzyme. For instance, in the presence of Mn(2+), it displays a specific Cys-Gly hydrolyzing activity of Cys-Gly-S-conjugates. Involved in the metabolism of glutathione and in the degradation of glutathione S-conjugates, which may play a role in the control of the cell redox status..
Function from UniProtKB (P28838), read 2026-09-23. CC BY 4.0.
Curated compounds routed: 0
332 statements
332 statements · 6 reference databases · Subject: LAP3 · Sources: Bgee, Hetionet, Human Protein Atlas, Human-GEM, Rhea, UniProt · Rows fetched: 300
6 reactions
L-cysteinylglycine+waterL-cysteine+glycine
Catalysed by LAP3 or NPEPPS or ANPEP
Reaction pageLeft to rightBalancedEC 3.4.11.1, 3.4.11.2cytosol
Human-GEM MAR04328CC BY 4.0Reference data
9 names
Resolves to: LAP3
Reaction pageLeft to rightBalancedEC 3.4.11.1, 3.4.11.2extracellular space
Human-GEM MAR04329CC BY 4.0Reference data
Catalysed by LAP3
Reaction pageLeft to rightBalancedEC 3.4.11.-cytosol
Human-GEM MAR07149CC BY 4.0Reference data
L-cysteinylglycine+waterL-cysteine+glycine
Reaction pageLeft to rightBalanced
Rhea RHEA:28783CC BY 4.0Reference data
an S-substituted L-cysteinylglycine+wateran S-substituted L-cysteine+glycine
Catalysed by LAP3
Reaction pageLeft to rightBalance undeterminable
Rhea RHEA:60444CC BY 4.0Reference data
S-benzyl-L-cysteinylglycine+waterS-benzyl-L-cysteine+glycine
Catalysed by LAP3
Reaction pageLeft to rightBalanced
Rhea RHEA:62568CC BY 4.0Reference data