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Entry
EC 3.4.24.18                Enzyme                                 

Name
meprin A;
endopeptidase-2;
meprin-a;
meprin;
N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase;
PABA-peptide hydrolase;
PPH
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Metalloendopeptidases
BRITE hierarchy
Reaction(IUBMB)
Hydrolysis of protein and peptide substrates preferentially on carboxyl side of hydrophobic residues
Comment
A membrane-bound metalloendopeptidase of rat and mouse kidney and intestinal brush borders, and salivary ducts. Differences from neprilysin (EC 3.4.24.11 (astacin family). Formerly included in EC 3.4.24.11
History
EC 3.4.24.18 created 1992
Orthology
K01395  
meprin A, alpha
K08606  
meprin A, beta
Genes
HSA: 
4224(MEP1A) 4225(MEP1B)
PTR: 
462745(MEP1A) 468515(MEP1B)
PPS: 
100991143(MEP1B) 100993933(MEP1A)
GGO: 
PON: 
100456833(MEP1A) 100461703(MEP1B)
MCC: 
704781(MEP1A) 707036(MEP1B)
MCF: 
102120570(MEP1B) 102141031(MEP1A)
MMU: 
17287(Mep1a) 17288(Mep1b)
RNO: 
25684(Mep1a) 25727(Mep1b)
CGE: 
100771501(Mep1a) 100774490(Mep1b)
HGL: 
101716131(Mep1a) 101721966(Mep1b)
TUP: 
102476731(MEP1A) 102501249(MEP1B)
CFA: 
481826(MEP1A) 490497(MEP1B)
AML: 
100467739(MEP1A) 100474827(MEP1B)
FCA: 
101089149(MEP1B) 101101056(MEP1A)
PTG: 
102969174(MEP1A) 102972887(MEP1B)
BTA: 
513936(MEP1A) 540701(MEP1B)
BOM: 
102270268(MEP1A) 102277511(MEP1B)
PHD: 
102318619(MEP1A) 102342891(MEP1B)
CHX: 
102181352(MEP1B) 102184856(MEP1A)
OAS: 
101114072(MEP1B) 101116774(MEP1A)
SSC: 
100154136(MEP1A) 100516141(MEP1B)
CFR: 
102509020(MEP1B) 102520791(MEP1A)
BACU: 
102999400(MEP1B) 103017419(MEP1A)
LVE: 
103087996(MEP1A) 103090304(MEP1B)
ECB: 
100052389(MEP1B) 100068383(MEP1A)
MYB: 
102251668(MEP1A) 102262211(MEP1B)
MYD: 
102754774(MEP1A) 102761324(MEP1B)
PALE: 
102878505(MEP1B) 102894555(MEP1A)
MDO: 
SHR: 
OAA: 
100080933(MEP1A) 100084811(MEP1B)
GGA: 
421097(MEP1B) 422060(MEP1A)
MGP: 
100545010(MEP1B) 100550277(MEP1A)
TGU: 
100223713(MEP1A) 100227825(MEP1B)
FAB: 
101810044(MEP1A) 101820401(MEP1B)
PHI: 
102106845(MEP1B) 102112290(MEP1A)
APLA: 
FPG: 
FCH: 
CLV: 
102093522(MEP1A) 102096310(MEP1B)
ASN: 
AMJ: 
PSS: 
102456515(MEP1B) 102462010(MEP1A)
CMY: 
102929325(MEP1A) 102938685(MEP1B)
ACS: 
PBI: 
103049257(MEP1B) 103066442(MEP1A)
XLA: 
XTR: 
100124942(mep1b) 548484(mep1a)
DRE: 
100151009(mep1b) 327586(fi19a06) 565535(mep1a.2)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
CMK: 
103191077(mep1b)
CIN: 
NVE: 
HMG: 
 » show all
Taxonomy
Reference
1  [PMID:7041888]
  Authors
Beynon RJ, Shannon JD, Bond JS.
  Title
Purification and characterization of a metallo-endoproteinase from mouse kidney.
  Journal
Biochem. J. 199 (1981) 591-8.
  Organism
Mus musculus
Reference
2  [PMID:3105525]
  Authors
Butler PE, McKay MJ, Bond JS.
  Title
Characterization of meprin, a membrane-bound metalloendopeptidase from mouse kidney.
  Journal
Biochem. J. 241 (1987) 229-35.
  Organism
Mus musculus
Reference
3  [PMID:2461706]
  Authors
Stephenson SL, Kenny AJ.
  Title
The metabolism of neuropeptides. Hydrolysis of peptides by the phosphoramidon-insensitive rat kidney enzyme 'endopeptidase-2' and by rat microvillar membranes.
  Journal
Biochem. J. 255 (1988) 45-51.
  Organism
Rattus norvegicus
Reference
4  [PMID:3261961]
  Authors
Sterchi EE, Naim HY, Lentze MJ, Hauri HP, Fransen JA.
  Title
N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase: a metalloendopeptidase of the human intestinal microvillus membrane which degrades biologically active peptides.
  Journal
Arch. Biochem. Biophys. 265 (1988) 105-18.
  Organism
Homo sapiens
Reference
5  [PMID:2690825]
  Authors
Barnes K, Ingram J, Kenny AJ.
  Title
Proteins of the kidney microvillar membrane. Structural and immunochemical properties of rat endopeptidase-2 and its immunohistochemical localization in tissues of rat and mouse.
  Journal
Biochem. J. 264 (1989) 335-46.
  Organism
Mus musculus, Rattus norvegicus
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
148938-24-3

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