3.4.21.109: matriptase

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For detailed information about matriptase, go to the full flat file.

Reaction

cleaves various synthetic substrates with Arg or Lys at the P1 position and prefers small side-chain amino acids, such as Ala and Gly, at the P2 position =

Synonyms

Epi/MTP, epithin, epithin/matriptase, influenza virus-activating protease, matriptase, matriptase-1, matriptase-2, matriptase-3, matriptase1, matriptase1a, membrane-type serine protease 1, membrane-type serine protease 1/matripase, membrane-type serine protease-1, membrane-type serine protease1, membrane-type serine proteinase matripase, membrane-type serine proteinase matriptase, More, MT-2, MT-SP-1, MT-SP1, MT-SP1/matripase, MT2, notopleural, prostamin, PRSS14, r-matripase, serine protease matriptase-2, serine protease SNC19/matripase, SNC19, ST-14, ST14, suppression of tumorigenecity 14, suppressor of tumorigenicity 14, suppressor of tumorigenicity 14 protein, suppressor of tumorigenicity-14, TADG-15, TADG15, TMPRSS6, transmembrane serine protease 6, tumor-associated differentially expressed gene-15, tumor-associated type II transmembrane serine protease, type 2 transmembrane serine protease, type II transmembrane protease, type II transmembrane serine protease

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.21 Serine endopeptidases

                3.4.21.109 matriptase

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Results	in table
32	Activating Compound
340	AA Sequence
23	Application
1	CAS Registry Number
48	Cloned(Commentary)
5	Crystallization (Commentary)
2424	Disease/ Diagnostics
11	Expression
55	General Information
2	General Stability
2	IC50 Value
292	Inhibitors
11	kcat/KM [mM/s]
232	Ki Value [mM]
61	KM Value [mM]
104	Localization
4	Metals/Ions
79	Molecular Weight [Da]
157	Natural Substrates/ Products (Substrates)
125	Organism
23	PDB ID
19	pH Optimum
1	pH Range
42	Posttranslational Modification
95	Protein Variants
23	Purification (Commentary)
9	Reaction
37	Reaction Type
122	Reference
3	Renatured (Commentary)
430	Source Tissue
3	Specific Activity [micromol/min/mg]
322	Substrates and Products (Substrate)
26	Subunits
193	Synonyms
13	Temperature Optimum [°C]
40	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.4.21.109 - matriptase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

complexed with benzamidine or bovine panreatic trypsin inhibitor, hanging drop vapor diffusion method

Homo sapiens

-

652266

in complex with inhibitor D-hTyr-Ala-4-amidinobenzylamide

Homo sapiens

Q9Y5Y6

754283

molecular docking of inhibitor. The P1 and P2 binding sites are occupied by the conserved Arg and then the variable second side chain, respectively. The 9-fluorenylmethyloxycarbonyl group forms pi-pi interactions with the conserved Trp in the P4 pocket

Homo sapiens

Q9Y5Y6

754402

mutant N164Q/R614A/S805A, to 2.5 A resolution. The structure of zymogen matriptase reveals a classical chymotrypsin-like zymogen fold

Homo sapiens

Q9Y5Y6

754183

purified recombinant refolded His-tagged matriptase catalytic domain in complex with benzamidine, 2-Nas-Phe(3-Am)-4-(2-guanidinoethyl)piperidide, and 4-([1-[(2S)-3-(3-carbamimidoylphenyl)-2-([[2,4,6-tris(1-methylethyl)phenyl]sulfonyl]amino)propanoyl]piperidin-4-yl]carbonyl)piperidine-1-carboximidamide, hanging drop vapor diffusion method, 18°C, 5 mg/mL matriptase, from 10 mM benzamidine, 0.1 M Tris-HCl, pH 8.5, 20% PEG 8000, and 200 mM MgCl2, X-ray diffraction structure determination and analysis at 2.1-2.2 A resolution

Homo sapiens

Q9Y5Y6

683753