Meprin A

Meprin A
Meprin A
Identifiers
Symbol	Meprin
InterPro	IPR008294
Membranome	537

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PMC	articles
PubMed	articles
NCBI	proteins

Meprin A
Meprin A
Identifiers
EC no.	3.4.24.18
CAS no.	148938-24-3
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
PMC
Search
PMC	articles
PubMed	articles
NCBI	proteins

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

meprin A, alpha

Identifiers

Symbol

Other data

Chr. 6 p12-p11

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Structures	Swiss-model
Domains	InterPro

meprin A, beta

Identifiers

Symbol

Other data

Chr. 18 q12.2-12.3

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Structures	Swiss-model
Domains	InterPro

References

^ 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.
^ ^a ^b 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. PMID 25617491.

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[pmid18783725-1] 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.

[Prox_2015-2] 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. PMID 25617491.

[1]

[2]

v t e Proteases: metalloendopeptidases (EC 3.4.24)
ADAM proteins	Alpha secretases ADAM9 ADAM10 ADAM17 ADAM19 ADAM2 ADAM7 ADAM8 ADAM11 ADAM12 ADAM15 ADAM18 ADAM22 ADAM23 ADAM28 ADAM33 ADAMTS1 ADAMTS2 ADAMTS3 ADAMTS4 ADAMTS5 ADAMTS8 ADAMTS9 ADAMTS10 ADAMTS12 ADAMTS13
Matrix metalloproteinases	Collagenases MMP1 MMP8 Gelatinases MMP2 MMP9 MMP3 MMP7 MMP10 MMP11 MMP12 MMP13 MMP14 MMP15 MMP16 MMP17 MMP19 MMP20 MMP21 MMP23A MMP23B MMP24 MMP25 MMP26 MMP27 MMP28
Other	Neprilysin Procollagen peptidase Thermolysin Pregnancy-associated plasma protein A Bone morphogenetic protein 1 Lysostaphin Insulin-degrading enzyme ZMPSTE24

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)