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Proteases, serine

Many enzymes have been the subject of protein engineering studies, including several that are important in medicine and industry, eg, lysozyme, trypsin, and cytochrome P450. SubtiHsin, a bacterial serine protease used in detergents, foods, and the manufacture of leather goods, has been particularly well studied (68). This emphasis is in part owing to the wealth of stmctural and mechanistic information that is available for this enzyme. [Pg.203]

Engineering Substrate Specificity. Although the serine proteases use a common catalytic mechanism, the enzymes have a wide variety of substrate specificities. For example, the natural variant subtiHsins of B. amyloliquefaciens (subtiHsin BPN J and B. licheniformis (subtiHsin Carlsberg) possess very similar stmctures and sequences where 86 of 275 amino acids are identical, but have different catalytic efficiencies, toward tetraamino acid -nitroanilide substrates (67). [Pg.203]

Table 3. Sequence Homologies for Serine Proteases Involved in Coagulation and Fibrinolysis ... Table 3. Sequence Homologies for Serine Proteases Involved in Coagulation and Fibrinolysis ...
Sequences have been determined for plasminogen and bovine Factor XII, and they are not homologous with the other serine proteases. The amino-terminal sequence of Factor XII is homologous, however, with the active site of several naturally occurring protease inhibitors (11). [Pg.173]

Coagulation Factors II, III, VII, IX, X, XI, and Xlla fragments, thrombin, and plasmin are classified as serine proteases because each possesses a serine residue with neighboring histidine and asparagine residues at its enzymatically active site (Table 3). Factors II, VII, IX, and X, Protein C, Protein S, and Protein Z are dependent on the presence of vitamin K [84-80-0] for their formation as biologically functionally active procoagulant glycoproteins. [Pg.173]

Factor II. Prothrombin is a vitamin K-dependent compound synthesized by the Hver. When prothrombin is activated it is cleaved at two sites, resulting in a two-chain molecule linked by a disulfide bond that has a molecular weight of 37,000 daltons. Thrombin is the serine protease that initiates the conversion of soluble fibrinogen into fibrin. [Pg.174]

Factor VII. This is a vitamin K-dependent serine protease that functions in the extrinsic coagulation pathway and catalyzes the activation of Factors IX and X. Factor VII is present constitutively in the surface membrane of pericytes and fibroblasts in the adventitia of blood vessels, vascular endothehum, and monocytes. It is a single-chain glycoprotein of approximately 50,000 daltons. [Pg.174]

Factor XI. Factor XI is a Hver-synthesized glycoprotein that circulates in a zymogen form as a dimer. It is converted to its active serine protease form by Factor Xlla in the presence of high molecular weight kininogen. Calcium is not required for this activation step. [Pg.174]

Protein G. This vitamin K-dependent glycoproteia serine protease zymogen is produced ia the Hver. It is an anticoagulant with species specificity (19—21). Proteia C is activated to Proteia by thrombomodulin, a proteia that resides on the surface of endothefial cells, plus thrombin ia the presence of calcium. In its active form, Proteia selectively iaactivates, by proteolytic degradation. Factors V, Va, VIII, and Villa. In this reaction the efficiency of Proteia is enhanced by complex formation with free Proteia S. la additioa, Proteia activates tissue plasminogen activator, which... [Pg.175]

Activated Proteia C (C ) [42617-41 -4] (19—21) is a aaturaHy occurring serine protease that, ia combination with free Proteia S, degrades and iaactivates Factors V, Va, VIII, and Villa. By degradation of these factors the blood becomes anticoagulated and thus may be a useful therapeutic agent. [Pg.178]

An example of a pseudoirreversible inhibitor has been demonstrated for chymotrypsin (36). This enzyme is a serine protease, and its mechanism of catalysis may be outlined as follows, where or R2 preferentially is a hydrophobic amino acid residue. [Pg.324]

J Greer. Comparative modelling methods Application to the family of the mammalian serine proteases. Proteins 7 317-334, 1990. [Pg.301]

Kraut, J. Serine proteases structure and mechanism of catalysis. Anna. Rev. Biochem. 46 331-358, 1977. [Pg.220]

Warshel, A., et al. How do serine proteases really work Biochemistry 28 3629-3637, 1989. [Pg.220]

Carter, P, Wells, J.A. Dissecting the catalytic triad of a serine protease. Nature 332 564-568, 1988. [Pg.220]

Grtitter, M.G., et al. Crystal structure of the thrombin-hirudin complex a novel mode of serine protease inhibition. EMBO J. 9 2361-2365, 1990. [Pg.220]

James, M.N.G., et al. Structures of product and inhibitor complexes of Streptomyces griseus protease A at 1.8 A resolution. A model for serine protease catalysis. [Pg.220]

Poulos, T.L., et al. Polypeptide halomethyl ketones bind to serine proteases as analogs of the tetrahedral intermediate. J. Biol. Chem. 251 1097-1103, 1976. [Pg.220]

Smith, S.O., et al. Crystal versus solution structures of enzymes NMR spectroscopy of a crystalline serine protease. Science 244 961-964, 1989. [Pg.221]

Sprang, S., et al. The three-dimensional structure of Asn ° mutant of trypsin role of Asp ° in serine protease catalysis. Science 237 905-909, 1987. [Pg.221]

Figure 16.21 Structure of one subunit of the core protein of Slndbls virus. The protein has a similar fold to chymotrypsin and other serine proteases, comprising two Greek key motifs separated by an active site cleft. The C-terminus of the protein is bound in the catalytic site, making the coat protein inactive (Adapted from S. Lee et al., Structure 4 531-541, 1996.)... Figure 16.21 Structure of one subunit of the core protein of Slndbls virus. The protein has a similar fold to chymotrypsin and other serine proteases, comprising two Greek key motifs separated by an active site cleft. The C-terminus of the protein is bound in the catalytic site, making the coat protein inactive (Adapted from S. Lee et al., Structure 4 531-541, 1996.)...
BLOOD CLOTTING. The formation of blood clots is the result of a series of zymogen activations (Figure 15.5). The amplification achieved by this cascade of enzymatic activations allows blood clotting to occur rapidly in response to injury. Seven of the clotting factors in their active form are serine proteases ... [Pg.464]


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Acetyl-enzyme from serine proteases

Activators serine proteases

Angiogenesis serine proteases

Aqualysin I Belongs to a Family of Subtilisin-type Serine Proteases

As serine protease

Blood clotting serine proteases

Blood coagulation role of serine protease

Bowman-Birk serine protease inhibitor

Bowman-Birk serine protease inhibitor ATI

Bowman-Birk serine protease inhibitor BTCIas

Bowman-Birk serine protease inhibitor CPTIsas

Bowman-Birk serine protease inhibitor D-IIas

Bowman-Birk serine protease inhibitor DATIas

Bowman-Birk serine protease inhibitor EBIas

Bowman-Birk serine protease inhibitor HGI-IIIas

Bowman-Birk serine protease inhibitor I (ABI

Bowman-Birk serine protease inhibitor bean)

Bowman-Birk serine protease inhibitor proteins

Catalytic cycles for serine protease

Catalytic triad of serine proteases

Chymotrypsin serine protease family

Cyclodextrin serine proteases

Digestion serine proteases

Effects of serine protease inhibitor

Endogenous serine protease inhibitors

Enzyme assay serine proteases

Enzyme serine protease inhibitor

Enzyme serine proteases

Enzymes serin protease

Inflammation serine proteases

Mammalian serine proteases

NMR spectra of serine proteases

Non-protein serine protease inhibitor from natural sources

Non-protein serine protease inhibitor phenolics

Non-protein serine protease inhibitor terpenes

Other Serine Proteases

Oxyanion hole of serine proteases

Pancreatic serine protease

Plant Kunitz serine protease inhibitor

Plant Kunitz serine protease inhibitor BASI (barley a-amylase

Plant Kunitz serine protease inhibitor Carica KPI

Plant Kunitz serine protease inhibitor Erythrina

Plant Kunitz serine protease inhibitor activator

Plant Kunitz serine protease inhibitor effects on ETI-a - plasminogen

Plant Kunitz serine protease inhibitor effects on Factor Xlla

Plant Kunitz serine protease inhibitor effects on Kallikrein

Plant Kunitz serine protease inhibitor effects on chymotrypsin

Plant Kunitz serine protease inhibitor effects on elastase

Plant Kunitz serine protease inhibitor effects on inferred KPI

Plant Kunitz serine protease inhibitor effects on subtilisin

Plant Kunitz serine protease inhibitor effects on subtilisin BPN

Plant Kunitz serine protease inhibitor effects on trypsin

Plant Kunitz serine protease inhibitor from Brassica napus

Plant Kunitz serine protease inhibitor from Glycine max

Plant Kunitz serine protease inhibitor from Hordeum vulgare

Plant Kunitz serine protease inhibitor from Ipomoea batatas

Plant Kunitz serine protease inhibitor from Lycopersicon esculentu

Plant Kunitz serine protease inhibitor from Nicotiana glauca

Plant Kunitz serine protease inhibitor from Nicotiana glutinosa

Plant Kunitz serine protease inhibitor from Oryza sativa

Plant Kunitz serine protease inhibitor from Populus deltoides

Plant Kunitz serine protease inhibitor from Prosopis juliflora

Plant Kunitz serine protease inhibitor from Psophocarpus

Plant Kunitz serine protease inhibitor proteinase

Plant Kunitz serine protease inhibitor proteins

Plant Kunitz serine protease inhibitor tetragonolobus

Plant serpins effects on serine protease

Plasma serine proteases

Platelet activation role of serine protease

Potato serine protease inhibitors

Potato type 1 serine protease

Potato type I serine protease inhibitor

Potato type I serine protease inhibitor Af4 gene product

Potato type I serine protease inhibitor effects on cathepsin

Potato type I serine protease inhibitor effects on chymotrypsin

Potato type II serine protease inhibitor

Potato type II serine protease inhibitor 6-domain PI precursor NaProPI

Potato type II serine protease inhibitor ARPIas

Potato type II serine protease inhibitor PCI-Ias

Potato type II serine protease inhibitor PTIas

Potato type II serine protease inhibitor Pepper leaf Pis

Potato type II serine protease inhibitor SaPIN2a SaPIN

Potato type II serine protease inhibitor aubergine

Potato type II serine protease inhibitor effects on Streptomyces griseus

Potato type II serine protease inhibitor effects on chymotrypsin

Potato type II serine protease inhibitor effects on pronase

Potato type II serine protease inhibitor effects on trypsin

Potato type II serine protease inhibitor from Capsicum annuum

Potato type II serine protease inhibitor from Lycopersicon esculentu

Potato type II serine protease inhibitor from Nicotiana alata

Potato type II serine protease inhibitor from Nicotiana alata (ornamental

Potato type II serine protease inhibitor from Nicotiana glutinosa

Potato type II serine protease inhibitor from Nicotiana tabacum

Potato type II serine protease inhibitor from Solanum tuberosum

Potato type II serine protease inhibitor proteinase

Potato type II serine protease inhibitor tobacco)

Prolyl endopeptidases serine proteases

Proprotein processing serine proteases

Proteins serine protease

Pulmonary vascular injury role of serine protease

Reaction of serine proteases

Sequences serine protease

Serin proteases

Serin proteases

Serine Proteases Minimal Schemes Catalytic Mechanisms Suicide Inhibition

Serine and Cysteine Proteases for Peptide Synthesis

Serine and cysteine proteases

Serine protease catalytic mechanisms

Serine protease cleavage sites

Serine protease elastase

Serine protease factor Vila inhibitors

Serine protease hydrolysis

Serine protease inactivation

Serine protease inhibition

Serine protease inhibitor

Serine protease inhibitor proteins

Serine protease inhibitor proteins inhibitors)

Serine protease inhibitors affinity labels

Serine protease mimetics

Serine protease prolyl

Serine protease prolyl endopeptidase

Serine protease prostate-specific antigen

Serine protease specificities

Serine protease structure

Serine protease suicide inhibition

Serine protease thrombin inhibitors

Serine protease urokinase

Serine protease with peptide

Serine protease with peptide chloromethyl ketone

Serine protease with peptide reaction

Serine protease zymogen

Serine protease, nucleophilicity

Serine proteases 3 sheet

Serine proteases active site

Serine proteases acyl-enzyme intermediates

Serine proteases amino acid

Serine proteases binding groups

Serine proteases blood clotting factors

Serine proteases carboxypeptidase

Serine proteases catalysis

Serine proteases catalytic activity

Serine proteases catalytic cycle

Serine proteases catalytic triad

Serine proteases cathepsin

Serine proteases chymase

Serine proteases chymotrypsin

Serine proteases classification

Serine proteases covalent intermediate

Serine proteases granzymes

Serine proteases in angiogenesis

Serine proteases in blood clotting

Serine proteases in cytosolic proteolysis

Serine proteases in digestion

Serine proteases in inflammation

Serine proteases in proprotein processing

Serine proteases in tissue remodelling

Serine proteases kallikrein

Serine proteases oxyanion hole

Serine proteases papain

Serine proteases pepsin

Serine proteases peptide synthesis

Serine proteases plasmin

Serine proteases products

Serine proteases protease inhibitors

Serine proteases residue

Serine proteases selectivities

Serine proteases stable derivatives

Serine proteases strategies

Serine proteases substrate binding

Serine proteases subtilisin

Serine proteases thrombin

Serine proteases trypsin

Serine proteases tryptase

Serine proteases urokinase type plasminogen

Serine proteases, calcium binding

Serine proteases, catalytic residues

Serine proteases, covalently bound

Serine-like proteases

Serpin, serine protease inhibitor

Specificity of serine proteases

Squash family serine protease inhibitor

Squash family serine protease inhibitor CPGTI

Squash family serine protease inhibitor Cucumis CMCTI

Squash family serine protease inhibitor Ecballium EETI

Squash family serine protease inhibitor LATIas

Squash family serine protease inhibitor LLDTI

Squash family serine protease inhibitor effects on Xa, Xlla, kallikrein

Squash family serine protease inhibitor effects on cathepsin

Squash family serine protease inhibitor effects on elastase

Squash family serine protease inhibitor effects on endopeptidase

Squash family serine protease inhibitor effects on trypsin

Squash family serine protease inhibitor from Bryonia dioica

Squash family serine protease inhibitor from Citrullus vulgaris

Squash family serine protease inhibitor from Cucumis melo

Squash family serine protease inhibitor from Cucumis sativus

Squash family serine protease inhibitor from Cucurbita maxima

Squash family serine protease inhibitor from Cucurbita pepo

Squash family serine protease inhibitor from Echinocystis lobata

Squash family serine protease inhibitor from Luffa acutangula

Squash family serine protease inhibitor from Luffa cylindrica

Squash family serine protease inhibitor from Momordica charanti

Squash family serine protease inhibitor from Momordica cochinchinensi

Squash family serine protease inhibitor from Momordica repens

Squash family serine protease inhibitor from Tricosanthes

Substrate of serine proteases

Substrate specificity of serine proteases

Subtilisin effects of serine protease inhibitor

Subtilisin-like serine protease

Subtilisin-type serine protease

The serine proteases

Tissue remodelling serine proteases

Trypsin-like serine protease factor

Trypsin-like serine protease, function

Trypsinlike serine protease

Urokinase type plasminogen activator serine proteases

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