Meprin A

Meprin A (EC 3.4.24.18, endopeptidase-2, meprin-a, meprin, N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase, PABA-peptide hydrolase, PPH) is an enzyme that cleaves protein and peptide substrates preferentially on carboxyl side of hydrophobic residues.[1] This metalloprotease can be associated with inflammatory responses.[2] It can be found in the extracellular space where it can also form complex structures by joining its monomers together.[2]

Meprin A
Identifiers
EC number3.4.24.18
CAS number148938-24-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Meprin A
Identifiers
SymbolMeprin
InterProIPR008294
Membranome537

Meprin A is a dimer composed of the products transcribed from the following two genes:

meprin A, alpha
Identifiers
SymbolMEP1A
NCBI gene4224
HGNC7015
OMIM600388
RefSeqNM_005588
UniProtQ16819
Other data
EC number3.4.24.18
LocusChr. 6 p12-p11
meprin A, beta
Identifiers
SymbolMEP1B
NCBI gene4225
HGNC7020
OMIM600389
RefSeqNM_005925
UniProtQ16820
Other data
EC number3.4.24.18
LocusChr. 18 q12.2-12.3

References
  1. Sterchi EE, Stöcker W, Bond JS (October 2008). "Meprins, membrane-bound and secreted astacin metalloproteinases". Molecular Aspects of Medicine. 29 (5): 309–28. doi:10.1016/j.mam.2008.08.002. PMC 2650038. PMID 18783725.
  2. Prox J, Arnold P, Becker-Pauly C (May 2015). "Meprin α and meprin β: procollagen proteinases in health and disease". Matrix Biology. 44: 7–13. doi:10.1016/j.matbio.2015.01.010.
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