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Search term: cell surface

<< < Results 201 - 297 of 297
EC Number Recommended Name Localization Commentary GeneOntology No. Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.11neprilysin cell surface - GO:0009986 AmiGO QuickGO 709805
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.13IgA-specific metalloendopeptidase cell surface - GO:0009986 AmiGO QuickGO 755335
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.13IgA-specific metalloendopeptidase cell surface associated via an N-terminal membrane anchor, release upon proteolytic cleavage GO:0009986 AmiGO QuickGO 666834
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.13IgA-specific metalloendopeptidase cell surface surface distribution of IgA1 protease on SS2 strain ZYS, overview GO:0009986 AmiGO QuickGO -, 754643
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.15thimet oligopeptidase cell surface - GO:0009986 AmiGO QuickGO -, 752926
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.15thimet oligopeptidase cell surface secretion to the medium GO:0009986 AmiGO QuickGO 683813
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.16neurolysin cell surface - GO:0009986 AmiGO QuickGO 683087
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.18meprin A cell surface - GO:0009986 AmiGO QuickGO 650462, 652104
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.23matrilysin cell surface - GO:0009986 AmiGO QuickGO 755514
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.23matrilysin cell surface extracellular MMP-7 binds to cell-surface cholesterol sulfate (CS) and acts as a membrane-associated protease GO:0009986 AmiGO QuickGO 754150
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.23matrilysin cell surface syndecan-2 functions as a cell surface docking receptor for pro-MMP-7, overview GO:0009986 AmiGO QuickGO 709073
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.23matrilysin cell surface the enzyme is secreted GO:0009986 AmiGO QuickGO 717801
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.23matrilysin cell surface the MMP-7 Asp137 genetic variant is preferentially localized to the cell surface plasma membrane GO:0009986 AmiGO QuickGO 708642
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.24gelatinase A cell surface besides MT-MMPs, which efficiently bind proMMP-2 to induce its activation, a limited number of cell-surface molecules have been shown to contribute to enhance proteolytic activity at the migrating front of invasive cells by clustering active MMP-2 at the cell membrane. Among them the heat shock protein HSP90a expressed at the surface of tumor cells promotes MMP-2 activity and tumor invasion by binding to the Hpx-like domain of MMP-2. The alphanybeta3 integrin is first identified as a binding site for the C-terminal Hpx-like domain of MMP-2 in studies investigating in vivo and in vitro interactions between angiogenic blood vessels and melanoma cells GO:0009986 AmiGO QuickGO 752865
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.24gelatinase A cell surface complex formed by MT1-MMP, TIMP-2 GO:0009986 AmiGO QuickGO 683846
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.34neutrophil collagenase cell surface binding of MMP-8 to the surface of polymorphonuclear cells promotes stability GO:0009986 AmiGO QuickGO 669709
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.35gelatinase B cell surface - GO:0009986 AmiGO QuickGO -, 708445
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.36leishmanolysin cell surface - GO:0009986 AmiGO QuickGO -, 683079, 683418, 683897
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.36leishmanolysin cell surface about two-thirds of newly synthesized enzyme becomes surface localized, the rest of enzyme does not reach the cell surface. Surface-localized enzyme is released at different rates from logarithmic and stationary phase virulent promastigotes. Major mechanism regulating enzyme abundance is the rate of loss of surface-localized enzyme from promastigote surface GO:0009986 AmiGO QuickGO 670182
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.36leishmanolysin cell surface GP63 is able to act on its substrate proteins within the nucleus of its host cell GO:0009986 AmiGO QuickGO 718304
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.36leishmanolysin cell surface major surface protein GO:0009986 AmiGO QuickGO -, 31226
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.36leishmanolysin cell surface surface molecules are glycosylphosphatidylinositol-anchored GO:0009986 AmiGO QuickGO 710519
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.36leishmanolysin cell surface two-third of MSPs in promastigotes is orientated along the cell surface, whereas most MSPs in amastigotes are localized in the flagellar pocket GO:0009986 AmiGO QuickGO -, 683857
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.56insulysin cell surface - GO:0009986 AmiGO QuickGO 683342, 710682
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.63meprin B cell surface - GO:0009986 AmiGO QuickGO -, 650462, 652104, 752709, 753172, 753218, 753321, 753536, 753697, 754028, 754236, 754779, 755294, 755466
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.71endothelin-converting enzyme 1 cell surface ECE-1 shedding from the surface of endothelial cells GO:0009986 AmiGO QuickGO 683474
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.71endothelin-converting enzyme 1 cell surface isozyme ECE-1c GO:0009986 AmiGO QuickGO 683435
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.79pappalysin-1 cell surface - GO:0009986 AmiGO QuickGO 735323
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.79pappalysin-1 cell surface detachment of pregnancy-associated plasma protein-A requires the formation of intermolecular proteinase-inhibitor disulfide bonds and glycosaminoglycan covalently bound to the inhibitor, mechanism, overview, the PAPP-A-proMBP complex is unable to bind to the cell surface GO:0009986 AmiGO QuickGO 683645
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.79pappalysin-1 cell surface surface association of PAPP-A accounts for its colocalization with activated macrophages in human atherosclerotic plaque, immunohistochemic analysis, overview GO:0009986 AmiGO QuickGO 683050
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.80membrane-type matrix metalloproteinase-1 cell surface - GO:0009986 AmiGO QuickGO 638809, 638810, 678111, 679042, 680921, 683787, 709058, 709415, 734409, 753242, 753773, 754158, 754175, 755435
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.80membrane-type matrix metalloproteinase-1 cell surface MT1-MMP forms a homophilic complex required for activity GO:0009986 AmiGO QuickGO 717536
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.80membrane-type matrix metalloproteinase-1 cell surface MT1-MMP on cell surface rapidly turns over by auto-degradation or clathrin-dependent internalization. MT1-MMP inactivated by TIMP-2 avoids auto-degradation, and accumulates on the cell surface, overview GO:0009986 AmiGO QuickGO 707998
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.81ADAM10 endopeptidase cell surface - GO:0009986 AmiGO QuickGO 667528, 668181, 668305, 668372, 668407
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.82ADAMTS-4 endopeptidase cell surface - GO:0009986 AmiGO QuickGO 669205, 697804
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.86ADAM 17 endopeptidase cell surface - GO:0009986 AmiGO QuickGO 638989, 638994, 638995, 639003, 639006
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.86ADAM 17 endopeptidase cell surface most mature ADAM17 is localised intracellularly, with only a small amount at the cell surface GO:0009986 AmiGO QuickGO 755446
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.87ADAMTS13 endopeptidase cell surface - GO:0009986 AmiGO QuickGO 713561
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.87ADAMTS13 endopeptidase cell surface ADAMTS13 binds to endothelial cells in a specific, reversible, and time-dependent manner with a Kd of 58 nM. Binding requires the COOH-terminal thrombospondin type 1 repeats of the protease. Binding is inhibited in the presence of heparin and by trypsin treatment of the cells GO:0009986 AmiGO QuickGO 712393
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.89Pro-Pro endopeptidase cell surface - GO:0009986 AmiGO QuickGO -, 754764
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.B10ADAM12 endopeptidase cell surface - GO:0009986 AmiGO QuickGO 668997, 755025
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.B11ADAMTS1 endopeptidase cell surface - GO:0009986 AmiGO QuickGO 697804
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.B12ADAMTS5 endopeptidase cell surface - GO:0009986 AmiGO QuickGO 679600, 697804
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.B14neprilysin-2 cell surface human neprilysin-2-beta is either localized to the extracellular surface or secreted GO:0009986 AmiGO QuickGO 733906
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.B28ADAM15 cell surface - GO:0009986 AmiGO QuickGO 735237
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.B9ADAM9 endopeptidase cell surface - GO:0009986 AmiGO QuickGO 754597
Show all pathways known for 3.5.1.19Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.19nicotinamidase cell surface surface location GO:0009986 AmiGO QuickGO 246587
Show all pathways known for 3.5.1.2Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.2glutaminase cell surface - GO:0009986 AmiGO QuickGO -, 656204, 719119
Show all pathways known for 3.5.1.2Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.2glutaminase cell surface of neutrophils, isozyme LGA GO:0009986 AmiGO QuickGO 670391
Show all pathways known for 3.5.1.24Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.24choloylglycine hydrolase cell surface - GO:0009986 AmiGO QuickGO -, 752522
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.28N-acetylmuramoyl-L-alanine amidase cell surface LytA is a surface-exposed enzyme GO:0009986 AmiGO QuickGO 656504
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.28N-acetylmuramoyl-L-alanine amidase cell surface recombinant PGRP-L shows primarily intracellular and cell surface location GO:0009986 AmiGO QuickGO 656179
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.41chitin deacetylase cell surface at early parasite life cycle GO:0009986 AmiGO QuickGO 668662
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.92pantetheine hydrolase cell surface - GO:0009986 AmiGO QuickGO -, 734537
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.92pantetheine hydrolase cell surface a glycosylphosphatidylinositol (GPI)-anchored ectoenzyme GO:0009986 AmiGO QuickGO 733009
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.92pantetheine hydrolase cell surface pantetheinase is an ectoenzyme that is attached to the outer plasma membrane by a glycosylphosphatidylinositol (GPI) anchor. GPI anchors consist of three domains: a phosphoethanolamine linker that attaches to the C terminal end of the target protein, a conserved glycan core and a phospholipid tail for anchoring to the lipid membrane GO:0009986 AmiGO QuickGO -, 756537
Display the word mapDisplay the reaction diagram Show all sequences 3.5.2.6beta-lactamase cell surface the class A beta-lactamase BlaC is a cell surface expressed serine hydrolase GO:0009986 AmiGO QuickGO -, 756194
Display the word mapDisplay the reaction diagram Show all sequences 3.5.3.15protein-arginine deiminase cell surface 90% of enzyme activity is cell surface associated GO:0009986 AmiGO QuickGO -, 733075
Show all pathways known for 3.6.1.15Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.15nucleoside-triphosphate phosphatase cell surface - GO:0009986 AmiGO QuickGO -, 756676, 758530
Show all pathways known for 3.6.1.22Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.22NAD+ diphosphatase cell surface - GO:0009986 AmiGO QuickGO 656433
Show all pathways known for 3.6.1.5Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.5apyrase cell surface - GO:0009986 AmiGO QuickGO -, 699181, 719597, 758530
Show all pathways known for 3.6.1.5Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.5apyrase cell surface NTPDase8 is a cell surface ectonucleotidase with a large extracellular domain containing the active site and is anchored to the membrane by two transmembrane domains at the N- and C-termini GO:0009986 AmiGO QuickGO 718863
Show all pathways known for 3.6.1.5Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.5apyrase cell surface the enzyme contains two transmembrane domains and five apyrase conserved regions, ACRs. ACR1 is located near the N-terminal transmembrane domain, whereas ACR5 is located near the C-terminal transmembrane domain GO:0009986 AmiGO QuickGO 695854
Show all pathways known for 3.6.1.9Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.9nucleotide diphosphatase cell surface - GO:0009986 AmiGO QuickGO 711034, 720186
Display the word mapDisplay the reaction diagram Show all sequences 3.6.5.2small monomeric GTPase cell surface - GO:0009986 AmiGO QuickGO 756101
Display the word mapDisplay the reaction diagram Show all sequences 3.6.5.5dynamin GTPase cell surface dynamin-1 GO:0009986 AmiGO QuickGO 669580
Display the word mapDisplay the reaction diagram Show all sequences 3.6.5.5dynamin GTPase cell surface dynamin-2 GO:0009986 AmiGO QuickGO 669580
Show all pathways known for 4.1.2.13Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.13fructose-bisphosphate aldolase cell surface - GO:0009986 AmiGO QuickGO -, 727893, 747043, 747971, 748619
Show all pathways known for 4.1.2.13Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.13fructose-bisphosphate aldolase cell surface surface-exposed enzyme GO:0009986 AmiGO QuickGO 748619
Show all pathways known for 4.2.1.1Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.1carbonic anhydrase cell surface - GO:0009986 AmiGO QuickGO 666801
Show all pathways known for 4.2.1.1Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.1carbonic anhydrase cell surface murine sperm possesses extracellular isozyme CA IV that is transferred to the sperm surface as the sperm pass through the epididymis, the transfer takes place in the corpus epididymidis GO:0009986 AmiGO QuickGO -, 716685
Show all pathways known for 4.2.1.11Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.11phosphopyruvate hydratase cell surface - GO:0009986 AmiGO QuickGO -, 651496, 666252, 696424, 698247, 704073, 704963, 705569, 706933, 715161, 730857
Show all pathways known for 4.2.1.11Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.11phosphopyruvate hydratase cell surface associated to the external surface of the parasite GO:0009986 AmiGO QuickGO 714875
Show all pathways known for 4.2.1.11Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.11phosphopyruvate hydratase cell surface putative ENOA translocation mechanism, overview GO:0009986 AmiGO QuickGO 714970
Show all pathways known for 4.2.1.11Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.11phosphopyruvate hydratase cell surface secreted enzyme associated to the external surface of the parasite GO:0009986 AmiGO QuickGO 714875
Display the word mapDisplay the reaction diagram Show all sequences 4.2.2.1hyaluronate lyase cell surface - GO:0009986 AmiGO QuickGO 664708, 666077, 680874
Display the word mapDisplay the reaction diagram Show all sequences 4.4.1.3dimethylpropiothetin dethiomethylase cell surface extracellular GO:0009986 AmiGO QuickGO -, 34604
Display the word mapDisplay the reaction diagram Show all sequences 5.2.1.8peptidylprolyl isomerase cell surface - GO:0009986 AmiGO QuickGO 680130
Display the word mapDisplay the reaction diagram Show all sequences 5.2.1.8peptidylprolyl isomerase cell surface enzymes EF0685 and EF1534 GO:0009986 AmiGO QuickGO 727618
Show all pathways known for 5.3.1.1Display the word mapDisplay the reaction diagram Show all sequences 5.3.1.1triose-phosphate isomerase cell surface - GO:0009986 AmiGO QuickGO -, 705563, 747934
Display the word mapDisplay the reaction diagram Show all sequences 5.3.4.1protein disulfide-isomerase cell surface - GO:0009986 AmiGO QuickGO 679122, 679424, 679678, 706459, 727573, 728220, 747835, 747836
Display the word mapDisplay the reaction diagram Show all sequences 5.6.1.6channel-conductance-controlling ATPase cell surface - GO:0009986 AmiGO QuickGO 734398
Show all pathways known for 6.1.1.17Display the word mapDisplay the reaction diagram Show all sequences 6.1.1.17glutamate-tRNA ligase cell surface - GO:0009986 AmiGO QuickGO 675229
Show all pathways known for 6.1.1.2Display the word mapDisplay the reaction diagram Show all sequences 6.1.1.2tryptophan-tRNA ligase cell surface - GO:0009986 AmiGO QuickGO 745941
Show all pathways known for 6.1.1.6Display the word mapDisplay the reaction diagram Show all sequences 6.1.1.6lysine-tRNA ligase cell surface the enzyme is exposed on the surface of stressed cells, on which it co-localized with calreticulin in lipid rafts GO:0009986 AmiGO QuickGO 714671
Show all pathways known for 7.1.2.2Display the word mapDisplay the reaction diagram Show all sequences 7.1.2.2H+-transporting two-sector ATPase cell surface - GO:0009986 AmiGO QuickGO 686272, 695945, 711983
Show all pathways known for 7.1.2.2Display the word mapDisplay the reaction diagram Show all sequences 7.1.2.2H+-transporting two-sector ATPase cell surface the ectopic expression of ATP synthase is a consequence of translocation from the mitochondria GO:0009986 AmiGO QuickGO 718469
Display the word mapDisplay the reaction diagram Show all sequences 7.2.2.12P-type Zn2+ transporter cell surface lipoprotein, detected by antibodies GO:0009986 AmiGO QuickGO 210345
Display the word mapDisplay the reaction diagram Show all sequences 7.2.2.19H+/K+-exchanging ATPase cell surface - GO:0009986 AmiGO QuickGO 687724
Display the word mapDisplay the reaction diagram Show all sequences 7.4.2.1ABC-type polar-amino-acid transporter cell surface - GO:0009986 AmiGO QuickGO 718559
Display the word mapDisplay the reaction diagram Show all sequences 7.4.2.14ABC-type antigen peptide transporter cell surface - GO:0009986 AmiGO QuickGO 761023
Display the word mapDisplay the reaction diagram Show all sequences 7.4.2.6ABC-type oligopeptide transporter cell surface - GO:0009986 AmiGO QuickGO 734416
Display the word mapDisplay the reaction diagram Show all sequences 7.4.2.6ABC-type oligopeptide transporter cell surface more than 80% of the surface-localised ATPase activity of Mycoplasma hominis is derived from OppA, implicating that OppA is the main ATPase on the surface of mycoplasma cells GO:0009986 AmiGO QuickGO 685829
Display the word mapDisplay the reaction diagram Show all sequences 7.4.2.6ABC-type oligopeptide transporter cell surface substrate binding protein OppA of the permease complex GO:0009986 AmiGO QuickGO 655869
Display the reaction diagram Show all sequences 7.4.2.7ABC-type alpha-factor-pheromone transporter cell surface enzyme variant with a deletion in the linker region GO:0009986 AmiGO QuickGO 670202
Display the word mapDisplay the reaction diagram Show all sequences 7.6.2.1P-type phospholipid transporter cell surface AP-1 is required, and GGA proteins, Golgi localized, gamma-ear containing, Arf-binding proteins acting as chlatrin adaptos, are dispensable, for efficient exclusion of Drs2p from exocytic vesicles targeted to the plasma membrane GO:0009986 AmiGO QuickGO 688911
Display the word mapDisplay the reaction diagram Show all sequences 7.6.2.2ABC-type xenobiotic transporter cell surface of tumor cells GO:0009986 AmiGO QuickGO 696241
<< < Results 201 - 297 of 297