metalloaminopeptidase activity

metalloaminopeptidase activity

Item
http://www.wikidata.org/entity/Q21097381
Alanyl (membrane) aminopeptidaseLeucyl/cystinyl aminopeptidaseThyrotropin releasing hormone degrading enzymeLaeverinLeukotriene A4 hydrolaseMatrix metallopeptidase 14Endoplasmic reticulum aminopeptidase 1Matrix metallopeptidase 15Matrix metallopeptidase 16Matrix metallopeptidase 17Methionyl aminopeptidase type 1D, mitochondrialArginyl aminopeptidase like 1X-prolyl aminopeptidase 2X-prolyl aminopeptidase 3X-prolyl aminopeptidase 1Methionyl aminopeptidase 2Endoplasmic reticulum aminopeptidase 2Aminopeptidase puromycin sensitiveMethionine aminopeptidase CTL0224Methionine aminopeptidase CT_851Aminopeptidase O (putative)Puromycin-sensitive aminopeptidase-like proteinAminopeptidase OMatrix metallopeptidase 16Arginyl aminopeptidase (aminopeptidase B)Methionine aminopeptidase BU230Aminopeptidase BB_0627Methionine aminopeptidase BB_0105Peptidase M24 family protein FTT_0609Methionine aminopeptidase FTT_0393Methionine aminopeptidase HP1299Methionine aminopeptidase PA3657Methionine aminopeptidase PA2748Methionine aminopeptidase TTHA1670Aminopeptidase QEndoplasmic reticulum aminopeptidase 1Glutamyl aminopeptidaseAspartyl aminopeptidaseMethionyl aminopeptidase 1Methionyl aminopeptidase type 1D (mitochondrial)
P680
Molecular cloning of the human kidney differentiation antigen gp160: human aminopeptidase AStructure of human cytosolic X-prolyl aminopeptidase: a double Mn(II)-dependent dimeric enzyme with a novel three-domain subunitcDNA cloning and expression of human glutamyl aminopeptidase (aminopeptidase A)Leukotriene A4 hydrolase/aminopeptidase. Glutamate 271 is a catalytic residue with specific roles in two distinct enzyme mechanismsStructural Insights into Central Hypertension Regulation by Human Aminopeptidase AThe low density lipoprotein receptor-related protein LRP is regulated by membrane type-1 matrix metalloproteinase (MT1-MMP) proteolysis in malignant cellsGenetic variation in the gene encoding calpain-10 is associated with type 2 diabetes mellitusPrion fragment peptides are digested with membrane type matrix metalloproteinases and acquire enzyme resistance through Cu²⁺-bindingAminopeptidase P3, a new member of the TNF-TNFR2 signaling complex, induces phosphorylation of JNK1 and JNK2.Structure of the human aminopeptidase XPNPEP3 and comparison of its in vitro activity with Icp55 orthologs: Insights into diverse cellular processes.
P921
Q14864891-D5416758-2763-4BCE-B8D7-84B55117E9F0Q14905507-B2C71FB2-F261-4CF7-A985-2116E3AF205CQ20180797-A3790F27-3697-486A-84E4-8748F80D9C57Q21097410-A5A4118B-06E6-44C4-B807-2056898F2F68Q21104634-A7A7DDED-7E08-4E85-A5C6-0F3D333A7654Q21109573-182476A8-563F-4AD5-A42A-19DEAF359E63Q21109573-3F3538C4-3179-485C-AD1D-7115AFF1974DQ21117696-47133B21-0B24-4150-B4F3-62F6E380B8F2Q21119465-7276FDAB-48F6-43A9-AFC6-F96C37CD931AQ21119466-501A6D0A-B178-4FD9-BAA9-5F3652289645Q21119466-BDFFE2B6-10AF-4E5D-AD15-D49F977C2F83Q21119478-D15D1426-22D9-49F9-8BFF-D1EE2080D1A9Q21119975-A2FEAAA9-F6AF-4F34-9769-B1C5FC4BDC14Q21122721-F40FD065-E6ED-44D0-8B2E-84EAF08B5ABFQ21123995-36ECDB96-D0E1-42B2-9D4F-95EF02A09F7AQ21123995-8948638D-334F-4EB6-A8E8-862A8926A469Q21124002-E82EB3BD-65E1-4319-AB59-7A1450E6FD5EQ21124003-328BB822-CCC7-47AE-95A7-F56AE9A5A7C9Q21124003-F22FEAA9-A561-41D5-9494-C80EFE3EBD58Q21130460-0CE60D72-D395-4B20-B81D-96A9F9A824C7Q21130620-C05BA42B-E973-422C-BDB8-F5369D64C9B5Q21134271-9F345CA9-DEE0-4B1B-A06A-8113C6C69059Q21172954-581311B8-2633-4CA2-8B1F-FEC4635493EBQ21174473-E2D13F21-7093-4516-B748-A61D24D62DE0Q21426146-79212980-6569-41B3-AA0F-3B015EB2F3A9Q21426146-EBC36576-D21F-4F65-A51C-5839173B9CB0Q21484182-F50DBDEA-527B-41C7-902C-B37A6F30C7CEQ21493873-747B5088-0E9D-408C-8B61-E86C7B5BFDE5Q21493873-874AC86E-2D62-49C4-AD0E-6747E9831D8EQ21496039-571F05AB-B7B7-45E8-A440-8D35CE7E07C6Q21496039-775BD83F-5D25-41D0-965B-4C9A8A881D2EQ21498968-B15612FB-A1B5-4D5B-973C-2D0A0A147E8CQ21498968-D9A4F89C-28AA-4187-A4AC-FD49EA2E841BQ21599732-14701D75-4DED-46CA-AC2A-AE5A02593326Q21603952-2CB7B289-DAE3-45AD-B079-A394E6B89F7BQ21604354-2F38885B-1876-4091-A4B7-87054E4CE88CQ21630161-EE1370AD-2E0F-4873-A1B4-0BAE12A3AC34Q21631486-7A79C420-89E6-4541-943A-17494CB39AFFQ21632394-F7A5B4DD-2675-4786-B76A-A3A73258A512Q21762113-3C708CF7-7F77-4D67-A046-18A07B7C7761
P680

metalloaminopeptidase activity

Item
http://www.wikidata.org/entity/Q21097381
description
Catalysis of the hydrolysis of ...... ide chains are ligands for the
@en
moleculaire functie
@nl
name
metalloaminopeptidase activity
@en
type
label
metalloaminopeptidase activity
@en
prefLabel
metalloaminopeptidase activity
@en
P279
P2888
P31
P686
P279
P2888
P31
P686