Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.5.1.4 (deaminase)
5,113 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Protease and basic amidase activity was found in the seminal plasma of the domestic turkey. Amidase activity, measured through use of N-alpha-benzoyl-DL-arginine-p-nitroanilide-HCL (BAPNA), was 23-28 times greater for turkey than for guinea fowl or chicken. Within the reproductive tract, seminal plasma from the vas deferens had much greater activity than testicular or epididymal fluids. Turkey seminal plasma enzyme (TSPE) purified by chromatography or isoelectric focusing showed three protein bands by PAGE, each resolving on SDS-PAGE into two subunits with molecular weights of approximately 28,000-32,000 and 38,000-44,000. One of the three proteins also contained a larger subunit (M(r) 76,000-81,000) thought to be transferrin. Turkey acrosin consisted of three subunits with molecular weights below 20,500. Acrosin, but not TSPE, was visualized in native gels with N-alpha-benzoyl-DL-arginine-beta-naphthylamide (BANA)/Fast Garnet stain. Michaelis constants (BAPNA) for TSPE, acrosin, and trypsin were 2.41 +/- 0.12 x 10(-4) M (n = 5), 4.96-6.03 x 10(-4) M (n = 2), and 6.76 +/- 0.95 x 10(-4) M (n = 6), respectively. TSPE, like acrosin and trypsin, was inhibited by benzamidine but not iodoacetamide. While all natural trypsin inhibitors tested inhibited acrosin, TSPE was not inhibited by ovomucoid from chicken or turkey egg white.
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PMID:Proteolytic enzymes in seminal plasma of domestic turkey (Meleagris gallopavo). 767 33

The N-end rule relates the in vivo half-life of a protein to the identity of its N-terminal residue. Tertiary destabilizing N-terminal residues asparagine and glutamine function through their conversion, by enzymatic deamidation, into the secondary destabilizing residues aspartate and glutamate, whose activity requires their enzymatic conjugation to arginine, one of the primary destabilizing residues. We isolated a Saccharomyces cerevisiae gene, termed NTA1, that encodes an amidase (Nt-amidase) specific for N-terminal asparagine and glutamine. Alterations at the putative active-site cysteine of the 52-kDa Nt-amidase inactivate the enzyme. Null nta1 mutants are viable but unable to degrade N-end rule substrates that bear N-terminal asparagine or glutamine. The effects of overexpressing Nt-amidase and other components of the N-end rule pathway suggest interactions between these components and the existence of a multienzyme targeting complex.
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PMID:Yeast N-terminal amidase. A new enzyme and component of the N-end rule pathway. 774 55

Among 29 strains of zygomycetes screened for serine carboxypeptidases, Absidia zychae NRIC 1199 showed the highest enzyme production. Two serine carboxypeptidases, CPZ-1 and CPZ-2, were purified to a homogeneous state from an extract of koji culture of A. zychae NRIC 1199. Purified CPZ-1 and CPZ-2 showed similar properties except the isoelectric point (pI); The pI of CPZ-1 and CPZ-2 were 4.50 and 4.65, respectively. The molecular weights of the CPZ-1 and CPZ-2 were 48,000 by SDS-PAGE and gel filtration. Among the proteinase inhibitors tested, phenylmethylsulfonyl fluoride and monoiodoacetic acid strongly inhibited the enzyme activity. The optimum pHs of CPZ-1 and CPZ-2 were 4.2 towards Z-Glu-Tyr. It is shown that the substrate specificities of CPZ-1 and CPZ-2 were dependent on the presence of bulky amino acid residues in the penultimate position (P1) for the small Z-peptides. However, in spite of the presence of Gly, Asp, Arg, or Pro in the P1 position, oligopeptides were hydrolyzed rapidly. CPZ-1 and CPZ-2 had not only carboxypeptidase but also carboxyamidase and amidase activities, and acted preferentially as a carboxyamidase for C-terminal amidated peptides. The hydrophobicity of P2 and P3 positions and the bulkiness of P1 and P'1 positions of the substrate may be important for carboxyamidase and amidase activities.
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PMID:Purification and characterization of serine carboxypeptidases from Absidia zychae. 776 58

Penicillin acylase (penicillin amidohydrolase, EC 3.5.1.11) is widely distributed among microorganisms, including bacteria, yeast and filamentous fungi. It is used on an industrial scale for the production of 6-aminopenicillanic acid, the starting material for the synthesis of semi-synthetic penicillins. Its in vivo role remains unclear, however, and the observation that expression of the Escherichia coli enzyme in vivo is regulated by both temperature and phenylacetic acid has prompted speculation that the enzyme could be involved in the assimilation of aromatic compounds as carbon sources in the organism's free-living mode. The mature E. coli enzyme is a periplasmic 80K heterodimer of A and B chains (209 and 566 amino acids, respectively) synthesized as a single cytoplasmic precursor containing a 26-amino-acid signal sequence to direct export to the cytoplasm and a 54-amino-acid spacer between the A and B chains which may influence the final folding of the chains. The N-terminal serine of the B chain reacts with phenylmethylsulphonyl fluoride, which is consistent with a catalytic role for the serine hydroxyl group. Modifying this serine to a cysteine inactivates the enzyme, whereas threonine, arginine or glycine substitution prevents in vivo processing of the enzyme, indicating that this must be an important recognition site for cleavage. Here we report the crystal structure of penicillin acylase at 1.9 A resolution. Our analysis shows that the environment of the catalytically active N-terminal serine of the B chain contains no adjacent histidine equivalent to that found in the serine proteases. The nearest base to the hydroxyl of this serine is its own alpha-amino group, which may act by a new mechanism to endow the enzyme with its catalytic properties.
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PMID:Penicillin acylase has a single-amino-acid catalytic centre. 781 45

Previous studies of amidase activity of human alpha-thrombin have yielded variable results and the decrease of this activity as a function of time and temperature has never been quantified. As this protease is an efficient tool in biochemistry and biotechnology thanks to its extreme selectivity, amidase activity and stability of thrombin were investigated with the synthetic substrate Tos-Gly-Pro-Arg-pNa. Enzyme activity as a function of temperature showed an optimum peak at 45 degrees C. The pH dependence of the activity showed a maximum around 9.5. The addition of NaCl promoted an increase of the activity. Stability of thrombin decreased rapidly when increasing the temperature from 25-45 degrees C and when diluting the enzyme. The presence of glycerol and ethylene glycol promoted a small increase of thrombin half life, whereas polyethylene glycol had a more pronounced positive effect even at very low concentrations.
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PMID:Amidase activity and thermal stability of human thrombin. 794 51

The fibrinolytic system was studied in normal human plasma containing increasing concentrations of acetone up to 23.4 mmol l-1. Fibrinolytic activity measured as euglobulin clot lysis time [ECLT] and amidase activities toward chromogenic peptide substrates H-D-Valyl-L-Leucyl-L-Lysine-p-nitroanilide 2 HCl [S-2251], designed for plasmin determination, H-D-Valyl-L-Phenylalanyl-L-Lysine-p-nitroanilide 2 HCl [S-2390], designed for the determination of t-PA in plasma via plasminogen activation and H-D-Prolyl-L-Phenyl-Alanyl-L-Arginine-p-nitro-anilide 2 HCl [S-2302], designed for the determination of kallikrein and activated Hageman factor, increased when 15.7 mmol l-1 concentration of acetone was reached. A parallel increase of esterolytic [substrate: naphthol-AS-acetate] activity was observed in euglobulin fractions. Crossed immunoelectrophoresis [CIE] revealed changes in fibrinogen profiles of plasma enriched with acetone as compared to native plasma. These findings suggest that acetone present in plasma in concentrations comparable to those found in some pathological states might activate fibrinolytic system.
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PMID:Enhancement of fibrinolytic activity of human plasma in the presence of acetone. 799 40

In this paper, we present the results of purification and characterization of an arginine/lysine amidase from the venom of Ophiophagus hannah (OhS1). It was purified by Sephadex G-75 gel filtration and ion-exchange chromatography on DEAE-Sepharose CL-6B. It is a protein of about 43,000, consisting of a single polypeptide chain. It is a minor component in the venom. The purified enzyme was capable of hydrolysing several tripeptidyl-p-nitroanilide substrates having either arginine or lysine as the C-terminal residue. We studied the kinetic parameters of OhS1 on six these chromogenic substrates. OhS1 did not clot fibrinogen. Electrophoresis of fibrinogen degraded with OhS1 revealed the disappearance of the alpha- and beta-chains and the appearance of lower mol. wt fragments. OhS1 had no hemorrhagic activity. It did not hydrolyse casein, nor did it act on blood coagulation factor X, prothrombin and plasminogen. The activity of OhS1 was completely inhibited by NPGB, PMSF, DFP, benzamidine and soybean trypsin inhibitor, suggesting it is a serine protease. Metal chelator (EDTA) had no effect on it.
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PMID:Characterization of OhS1, an arginine/lysine amidase from the venom of king cobra (Ophiophagus hannah). 807 73

Two forms of acidic arginine amidases were separated from human kidney extract using the techniques of basic ion exchange adsorption and elution as well as lima bean trypsin inhibitor (LBTI) and aprotinin affinity adsorptions and elutions. The enzymes were tentatively named acidic human renal arginine amidase-L (AHRAA-L, with affinity to an LBTI column) and -A (AHRAA-A, with affinity to an aprotinin column). Both enzymes showed a similar molecular mass of approximately 3.0 x 10(4) daltons, differing from that of human renal kallikrein (HRK, molecular mass of 4.8 x 10(4) daltons). The specific activity of AHRAA-L and -A were 106 and 680 nmol/min/A280 of Val-Leu-Arg-pNA amidolysis, respectively, and they were strongly inhibited by LBTI and human urinary trypsin inhibitor (UTI), while ethylenglycol-bis(beta-amino ethylether)-N,N,N',N'-tetraacetic acid (EGTA) showed a weak or no effect on both enzymes.
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PMID:Two forms of acidic arginine amidases in human kidney. 813 42

Urea is a time-dependent active-site-directed inhibitor of Pseudomonas aeruginosa amidase. We found that 20 mM hydroxylamine caused bound urea to be released from the inactive urea:amidase complex with the restoration of enzyme activity. Bound urea restricts the titrability of the enzyme's -SH groups to 6 per hexameric molecule and protects it against thermal denaturation suggesting that urea binding provokes a conformational change in the enzyme. Mutations in the P. aeruginosa amidase gene that reduce the binding affinity of the enzyme for both urea and the substrate acetamide have been identified by direct sequencing of PCR-amplified mutant genes and confirmed by sequencing cloned PCR-amplified genes. The mutations were in two regions of the enzyme substituting either Arg-188 (or Gln-190, in one case) or Trp-144; one amidase that bound neither urea nor acetamide was doubly mutant with an amino-acid change at both sites.
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PMID:Arg-188 and Trp-144 are implicated in the binding of urea and acetamide to the active site of the amidase from Pseudomonas aeruginosa. 814 78

The effects of zona pellucida glycoproteins, sulfated polymers and non-sulfated polymers on the activation kinetics of boar sperm proacrosin to beta-acrosin have been investigated. The aim has been to understand more about the behaviour and function of this protein after it has been released from the acrosome at the time of fertilization. Purified proacrosin was allowed to autoactivate at pH 8.0 in the presence of different concentrations of homologous zona glycoproteins, sulfated polymers (fucoidan, chondroitin sulfates A, B and C, dextran sulfate, polyvinylsulfate and heparin) and non-sulfated polymers (dextran, polyvinylphosphate and hyaluronic acid). Enzyme activity was measured against N-benzoyl-L-arginine p-nitroanalide substrate and changes in molecular mass of the protein monitored by SDS-PAGE. Results show that zona pellucida glycoproteins, fucoidan, dextran sulfate and polyvinylsulfate all potentiate the conversion of proacrosin to beta-acrosin but subsequently inhibit its amidase activity. Dextran, polyvinylphosphate, chondroitin sulfates A, B and C and glucose-6-sulfate, on the other hand, either have no effect on autoactivation and beta-acrosin activity, or enhance it slightly. SDS-PAGE analysis confirmed these observations and further indicated that binding of sulfated polymers to proacrosin inhibited staining by Coomassie Blue. These results are consistent with the hypothesis that binding of zona pellucida glycoproteins and sulfated compounds to proacrosin/acrosin is stereospecific and that contact activation onto soluble 'surfaces' causes conformational changes that are responsible for potentiation or inhibition of activation. The implications of these findings for sperm binding and penetration of the zona pellucida are discussed.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Some effects of zona pellucida glycoproteins and sulfated polymers on the autoactivation of boar sperm proacrosin and activity of beta-acrosin. 818 87


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