Summary for peptidase M01.003: aminopeptidase A

Summary Gene structure Alignment Tree Sequences Sequence features Distribution Structure Literature Human EST Mouse EST Substrates Inhibitors Pharma

 

Names
MEROPS Nameaminopeptidase A
Other namesangiotensinase A, aspartate aminopeptidase, Ca2+-activated glutamate aminopeptidase, ENPEP g.p. (Homo sapiens), glutamyl aminopeptidase, glutamyl peptidase, gp160 [ambig.], membrane aminopeptidase II, mouse BP-1/6C3 antigen, rhiminopeptidase A (Bitis gabonica)
Domain architecture
MEROPS Classification
Classification Clan MA >> Subclan MA(E) >> Family M1 >> Subfamily (none) >> M01.003
Holotypeaminopeptidase A (Homo sapiens), Uniprot accession Q07075 (peptidase unit: 304-520), MERNUM MER0001012
History Identifier created: Handbook of Proteolytic Enzymes (1998) Academic Press, London.
Activity
Catalytic typeMetallo
PeplistIncluded in the Peplist with identifier PL00125
NC-IUBMBSubclass 3.4 (Peptidases) >> Sub-subclass 3.4.11 (Aminopeptidases) >> Peptidase 3.4.11.7
EnzymologyBRENDA database
Proteolytic eventsCutDB database (3 cleavages)
Activity statushuman: active (Wang & Cooper, 2004)
mouse: active (Vazeux et al., 1997)
PhysiologyEctoenzyme degrading angiotensin II.
KnockoutMice homozygous for deficiency of the enzyme developed normally, generated normal numbers of T and B cells, exhibited normal antibody responses to both thymus-dependent and -independent antigens, and showed normal serum immunoglobulin levels. It was therefore concluded that the enzyme is not essential for normal B and T cell development (Lin et al., 1998). However, although the deficient mice developed normally, they failed to mount the expected angiogenic response to hypoxia or growth factors (Marchio et al., 2004).
Pharmaceutical relevanceAminopeptidase A is involved in the formation of brain angiotensin III, which exerts a tonic stimulatory action on the central control of blood pressure. Thus, central inhibitors of aminopeptidase A constitute putative central antihypertensive agents (Rozenfeld et al., 2002; Fournie-Zaluski et al., 2004). The enzyme also is a regulator of blood vessel formation, and is a putative target for angiogenesis in cancer.
Pathways KEGGRenin-angiotensin system
Other databases WIKIPEDIAhttp://en.wikipedia.org/wiki/Glutamyl_aminopeptidase
Cleavage site specificity Explanations of how to interpret the following cleavage site sequence logo and specificity matrix can be found here.
Cleavage pattern-/-/-/EdScissile bonde/-/-/- (based on 14 cleavages)
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Specificity matrix
 
Amino acid P4 P3 P2 P1 P1' P2' P3' P4'
Gly 0 0 0 0 0 0 1 1
Pro 0 0 0 0 0 1 1 0
Ala 0 0 0 0 0 1 1 1
Val 0 0 0 0 1 1 1 2
Leu 0 0 0 0 0 0 0 0
Ile 0 0 0 0 0 0 1 1
Met 0 0 0 1 2 2 1 1
Phe 0 0 0 0 0 0 1 2
Tyr 0 0 0 0 1 1 1 0
Trp 0 0 0 0 0 0 0 1
Ser 0 0 0 0 0 0 0 0
Thr 0 0 0 0 0 0 0 0
Cys 0 0 0 0 0 0 0 0
Asn 0 0 0 0 0 0 0 0
Gln 0 0 0 0 0 0 0 0
Asp 0 0 0 4 0 1 1 0
Glu 0 0 0 7 4 3 2 1
Lys 0 0 0 1 0 0 0 0
Arg 0 0 0 1 2 0 0 0
His 0 0 0 0 1 1 0 1
Human genetics
Gene symbol Locus Megabases Ensembl Entrez gene Gene Cards OMIM
ENPEP 4q25 ENSG00000138792 2028 ENPEP 138297
Mouse genetics
Gene symbol Position Megabases Ensembl Entrez gene MGI
Enpep 3:G3 ENSMUSG00000028024 13809 MGI:106645