about
Angiotensin I converting enzymeAngiotensin I converting enzyme (peptidyl-dipeptidase A) 1Carboxypeptidase QCarboxypeptidase QCarboxypeptidase QDipeptidase 1Peptidase T VCA0180Acetylornithine deacetylase VC2645Aminoacyl-histidine dipeptidase HI0675Aminoacyl-histidine dipeptidase BT_1615Aminoacyl-histidine dipeptidase BT_4045Aminoacyl-histidine dipeptidase FN1804Aminoacyl-histidine dipeptidase FN1408Aminoacyl-histidine dipeptidase FN1277Aminoacyl-histidine dipeptidase BC2439Amidohydrolase CBO1431Cytosol nonspecific dipeptidase STM0316Aminoacyl-histidine/glycine-aspartate dipeptidase PepD SO_1115Peptidase M28D family SO_3539Metallodipeptidase YFR044CDipeptidase 1Carboxypeptidase QDipeptidase 1Carboxypeptidase QDipeptidase 1Carboxypeptidase Q
P680
Purification, cDNA cloning, and expression of a new human blood plasma glutamate carboxypeptidase homologous to N-acetyl-aspartyl-alpha-glutamate carboxypeptidase/prostate-specific membrane antigenDipeptide hydrolysis by the dinuclear zinc enzyme human renal dipeptidase: mechanistic insights from DFT calculationsThe two homologous domains of human angiotensin I-converting enzyme are both catalytically activeAngiotensin I-converting enzyme mutation (Trp1197Stop) causes a dramatic increase in blood ACEExpression and characterization of recombinant human angiotensin I-converting enzyme. Evidence for a C-terminal transmembrane anchor and for a proteolytic processing of the secreted recombinant and plasma enzymesCatalysis of angiotensin I hydrolysis by human angiotensin-converting enzyme: effect of chloride and pH
P921
Q128861-4E888BA2-4371-4980-83CD-4EE9CFF80979Q14864000-626A879D-F3F3-492A-88DC-E632D7BCDBF3Q21131187-13B0543B-5D60-4E84-A4E4-555F7B5475C6Q21131187-CA021954-2DB4-424F-982D-0FE9E8FFBFB5Q21151408-AB015DB3-3FA7-4EFC-B954-F2D66239D89AQ21498083-074B8FB3-0773-4C33-ABDF-10F2135B371FQ21498083-73134156-4A03-46A7-9BAC-B5E3FA7A73B6Q21981546-DA77975D-F63F-4996-9EE1-1896116B51CBQ23435668-EE7BC00E-6100-4EDE-9015-2E51DA74719FQ23435873-5760745D-6A9C-4881-A4AD-51C996D43FCCQ23445321-D85E3BF2-DB3E-4255-9C10-980DF64B1D42Q23455417-D2F58589-DCC1-4DFB-8038-41CA3B47A20BQ23455684-79757A48-2085-411B-BD60-590CACD241CFQ23458927-96DF8B00-0063-4D07-8550-AA250ADFD77FQ23459016-E6032101-7C39-47F8-ABA0-67AF2A361A85Q23460881-B905C914-211B-49A5-AE17-55A58B22CA4FQ23514293-EC941669-847C-4184-938D-4E1D82809BBEQ23530211-FF98CB3D-9D28-42FA-A515-570DC4996250Q23559590-6F900179-05EF-433B-A609-36A9B09C9569Q23599618-E4956FBD-B648-4F2C-A687-74C47C38BE0FQ23599986-D4C05B45-9B35-40D7-A589-88B954FC705FQ27550486-5DD27684-4973-4455-8732-2A491F835D1FQ28556153-D9083675-FF4B-4FEE-B724-9B5EF668B733Q28556580-12D42F54-F497-4F38-9702-CAC4B6ED38C1Q5279726-1666F621-43AE-4BF1-9C1A-8C7B4286A919Q55204570-8A5663CC-2064-4C8B-894F-F22DBF9FA369Q55204807-EA5F6285-3C90-4065-A920-098C9C89A305Q59251771-E895A1A0-DCA8-4E9E-AF62-EA969137F679
P680
description
Catalysis of the hydrolysis of ...... re ligands for the metal ions.
@en
moleculaire functie
@nl
name
metallodipeptidase activity
@en
type
label
metallodipeptidase activity
@en
altLabel
GO:0070573
@en
metallo-exo-dipeptidase activity
@en
metalloexodipeptidase activity
@en
prefLabel
metallodipeptidase activity
@en
P2888
P686
GO:0070573