3.4.24.11 neprilysin cell surface - 9986 709805 3.4.24.13 IgA-specific metalloendopeptidase cell surface - 9986 755335 3.4.24.13 IgA-specific metalloendopeptidase cell surface associated via an N-terminal membrane anchor, release upon proteolytic cleavage 9986 666834 3.4.24.13 IgA-specific metalloendopeptidase cell surface surface distribution of IgA1 protease on SS2 strain ZYS, overview 9986 -, 754643 3.4.24.15 thimet oligopeptidase cell surface - 9986 -, 752926 3.4.24.15 thimet oligopeptidase cell surface secretion to the medium 9986 683813 3.4.24.16 neurolysin cell surface - 9986 683087 3.4.24.18 meprin A cell surface - 9986 650462, 652104 3.4.24.23 matrilysin cell surface - 9986 755514 3.4.24.23 matrilysin cell surface extracellular MMP-7 binds to cell-surface cholesterol sulfate (CS) and acts as a membrane-associated protease 9986 754150 3.4.24.23 matrilysin cell surface syndecan-2 functions as a cell surface docking receptor for pro-MMP-7, overview 9986 709073 3.4.24.23 matrilysin cell surface the enzyme is secreted 9986 717801 3.4.24.23 matrilysin cell surface the MMP-7 Asp137 genetic variant is preferentially localized to the cell surface plasma membrane 9986 708642 3.4.24.24 gelatinase 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 9986 752865 3.4.24.24 gelatinase A cell surface complex formed by MT1-MMP, TIMP-2 9986 683846 3.4.24.34 neutrophil collagenase cell surface binding of MMP-8 to the surface of polymorphonuclear cells promotes stability 9986 669709 3.4.24.35 gelatinase B cell surface - 9986 -, 708445 3.4.24.36 leishmanolysin cell surface - 9986 -, 683079, 683418, 683897 3.4.24.36 leishmanolysin 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 9986 670182 3.4.24.36 leishmanolysin cell surface GP63 is able to act on its substrate proteins within the nucleus of its host cell 9986 718304 3.4.24.36 leishmanolysin cell surface major surface protein 9986 -, 31226 3.4.24.36 leishmanolysin cell surface surface molecules are glycosylphosphatidylinositol-anchored 9986 710519 3.4.24.36 leishmanolysin 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 9986 -, 683857 3.4.24.56 insulysin cell surface - 9986 683342, 710682 3.4.24.63 meprin B cell surface - 9986 -, 650462, 652104, 752709, 753172, 753218, 753321, 753536, 753697, 754028, 754236, 754779, 755294, 755466 3.4.24.71 endothelin-converting enzyme 1 cell surface ECE-1 shedding from the surface of endothelial cells 9986 683474 3.4.24.71 endothelin-converting enzyme 1 cell surface isozyme ECE-1c 9986 683435 3.4.24.79 pappalysin-1 cell surface - 9986 735323 3.4.24.79 pappalysin-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 9986 683645 3.4.24.79 pappalysin-1 cell surface surface association of PAPP-A accounts for its colocalization with activated macrophages in human atherosclerotic plaque, immunohistochemic analysis, overview 9986 683050 3.4.24.80 membrane-type matrix metalloproteinase-1 cell surface - 9986 638809, 638810, 678111, 679042, 680921, 683787, 709058, 709415, 734409, 753242, 753773, 754158, 754175, 755435 3.4.24.80 membrane-type matrix metalloproteinase-1 cell surface MT1-MMP forms a homophilic complex required for activity 9986 717536 3.4.24.80 membrane-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 9986 707998 3.4.24.81 ADAM10 endopeptidase cell surface - 9986 667528, 668181, 668305, 668372, 668407 3.4.24.82 ADAMTS-4 endopeptidase cell surface - 9986 669205, 697804 3.4.24.86 ADAM 17 endopeptidase cell surface - 9986 638989, 638994, 638995, 639003, 639006 3.4.24.86 ADAM 17 endopeptidase cell surface most mature ADAM17 is localised intracellularly, with only a small amount at the cell surface 9986 755446 3.4.24.87 ADAMTS13 endopeptidase cell surface - 9986 713561 3.4.24.87 ADAMTS13 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 9986 712393 3.4.24.89 Pro-Pro endopeptidase cell surface - 9986 -, 754764 3.4.24.B10 ADAM12 endopeptidase cell surface - 9986 668997, 755025 3.4.24.B11 ADAMTS1 endopeptidase cell surface - 9986 697804 3.4.24.B12 ADAMTS5 endopeptidase cell surface - 9986 679600, 697804 3.4.24.B14 neprilysin-2 cell surface human neprilysin-2-beta is either localized to the extracellular surface or secreted 9986 733906 3.4.24.B28 ADAM15 cell surface - 9986 735237 3.4.24.B9 ADAM9 endopeptidase cell surface - 9986 754597 3.5.1.19 nicotinamidase cell surface surface location 9986 246587 3.5.1.2 glutaminase cell surface - 9986 -, 656204, 719119 3.5.1.2 glutaminase cell surface of neutrophils, isozyme LGA 9986 670391 3.5.1.24 choloylglycine hydrolase cell surface - 9986 -, 752522 3.5.1.28 N-acetylmuramoyl-L-alanine amidase cell surface LytA is a surface-exposed enzyme 9986 656504 3.5.1.28 N-acetylmuramoyl-L-alanine amidase cell surface recombinant PGRP-L shows primarily intracellular and cell surface location 9986 656179 3.5.1.41 chitin deacetylase cell surface at early parasite life cycle 9986 668662 3.5.1.92 pantetheine hydrolase cell surface - 9986 -, 734537 3.5.1.92 pantetheine hydrolase cell surface a glycosylphosphatidylinositol (GPI)-anchored ectoenzyme 9986 733009 3.5.1.92 pantetheine 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 9986 -, 756537 3.5.2.6 beta-lactamase cell surface the class A beta-lactamase BlaC is a cell surface expressed serine hydrolase 9986 -, 756194 3.5.3.15 protein-arginine deiminase cell surface 90% of enzyme activity is cell surface associated 9986 -, 733075 3.6.1.15 nucleoside-triphosphate phosphatase cell surface - 9986 -, 756676, 758530 3.6.1.22 NAD+ diphosphatase cell surface - 9986 656433 3.6.1.5 apyrase cell surface - 9986 -, 699181, 719597, 758530 3.6.1.5 apyrase 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 9986 718863 3.6.1.5 apyrase 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 9986 695854 3.6.1.9 nucleotide diphosphatase cell surface - 9986 711034, 720186 3.6.5.2 small monomeric GTPase cell surface - 9986 756101 3.6.5.5 dynamin GTPase cell surface dynamin-1 9986 669580 3.6.5.5 dynamin GTPase cell surface dynamin-2 9986 669580 4.1.2.13 fructose-bisphosphate aldolase cell surface - 9986 -, 727893, 747043, 747971, 748619 4.1.2.13 fructose-bisphosphate aldolase cell surface surface-exposed enzyme 9986 748619 4.2.1.1 carbonic anhydrase cell surface - 9986 666801 4.2.1.1 carbonic 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 9986 -, 716685 4.2.1.11 phosphopyruvate hydratase cell surface - 9986 -, 651496, 666252, 696424, 698247, 704073, 704963, 705569, 706933, 715161, 730857 4.2.1.11 phosphopyruvate hydratase cell surface associated to the external surface of the parasite 9986 714875 4.2.1.11 phosphopyruvate hydratase cell surface putative ENOA translocation mechanism, overview 9986 714970 4.2.1.11 phosphopyruvate hydratase cell surface secreted enzyme associated to the external surface of the parasite 9986 714875 4.2.2.1 hyaluronate lyase cell surface - 9986 664708, 666077, 680874 4.4.1.3 dimethylpropiothetin dethiomethylase cell surface extracellular 9986 -, 34604 5.2.1.8 peptidylprolyl isomerase cell surface - 9986 680130 5.2.1.8 peptidylprolyl isomerase cell surface enzymes EF0685 and EF1534 9986 727618 5.3.1.1 triose-phosphate isomerase cell surface - 9986 -, 705563, 747934 5.3.4.1 protein disulfide-isomerase cell surface - 9986 679122, 679424, 679678, 706459, 727573, 728220, 747835, 747836 5.6.1.6 channel-conductance-controlling ATPase cell surface - 9986 734398 6.1.1.17 glutamate-tRNA ligase cell surface - 9986 675229 6.1.1.2 tryptophan-tRNA ligase cell surface - 9986 745941 6.1.1.6 lysine-tRNA ligase cell surface the enzyme is exposed on the surface of stressed cells, on which it co-localized with calreticulin in lipid rafts 9986 714671 7.1.2.2 H+-transporting two-sector ATPase cell surface - 9986 686272, 695945, 711983 7.1.2.2 H+-transporting two-sector ATPase cell surface the ectopic expression of ATP synthase is a consequence of translocation from the mitochondria 9986 718469 7.2.2.12 P-type Zn2+ transporter cell surface lipoprotein, detected by antibodies 9986 210345 7.2.2.19 H+/K+-exchanging ATPase cell surface - 9986 687724 7.4.2.1 ABC-type polar-amino-acid transporter cell surface - 9986 718559 7.4.2.14 ABC-type antigen peptide transporter cell surface - 9986 761023 7.4.2.6 ABC-type oligopeptide transporter cell surface - 9986 734416 7.4.2.6 ABC-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 9986 685829 7.4.2.6 ABC-type oligopeptide transporter cell surface substrate binding protein OppA of the permease complex 9986 655869 7.4.2.7 ABC-type alpha-factor-pheromone transporter cell surface enzyme variant with a deletion in the linker region 9986 670202 7.6.2.1 P-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 9986 688911 7.6.2.2 ABC-type xenobiotic transporter cell surface of tumor cells 9986 696241