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:3.4.25.1 (proteasome)
28,817 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. The inhibitory activity of an alkaline protease inhibitor, (Streptomyces subtilisin inhibitor) towards subtilisin is found to decrease by photooxidation sensitized by methylene blue with a clear pH dependence, the midpoint of which is about 6.0. 2. Amino acid analyses of photooxidized Streptomyces subtilisin inhibitor indicate that one of the two histidyl residues and the three methionyl residues are destroyed, concomittant with the loss of inhibitory activity. 3. In accordance with this observation, one of the clearly resolved nuclear magnetic resonances from C2-protons of the two histidyl residues is selectively diminished. This histidyl residue, sensitive to photooxidation and giving a proton magnetic resonance peak at lower field, is assigned to His-106 from peptide analyses. 4. Independent modification of methionyl residues by a reaction with H2O2 or Cl2 also decreases the inhibitory activity of Streptomyces subtilisin inhibitor. 5. Modification of lysyl, tyrosyl and tryptophanyl residues by diazonium-1-H-tetrazole does not lead to the loss of the inhibitory activity. 6. The above results indicate that one or more methionyl residue(s) are essential to the inhibitory activity of Streptomyces subtilisin inhibitor, whereas lysyl, tyrosyl and tryptophanyl residues are not essential to the inhibitory activity. Modification of His-106 is also strongly related to the loss of activity, although its distinct participation in the inactivation mechanism has not been demonstrated.
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PMID:Inactivation of Streptomyces subtilisin inhibitory by chemical modifications. 1 22

The effect of glucose and amino acids on the synthesis of alkaline protease of the prototroph strain and auxotrophs of Bacillus subtilis A-50 was studied. There are both general and different from one another mechanisms of regulation for sporulation and protease synthesis as one of early stages of sporulation. Most auxotroph mutations pleiotropically decrease the level of protease synthesis and the efficiency of sporulation. At the same time the differences depending on sporulation and protease formation from glucose, amino acids and caseinoacids are observed. The increase in glucose concentration in the medium from 0.5 to 5% leads to intensification of protease synthesis and decrease of the sporulation efficiency. The suppression of alkaline protease formation in B. subtilis occurs when amino acid concentration is of the order of 1.5 mg/ml in the studied combination in the presence of 1--5% glucose. The strongest inhibitory effect was discovered for 2d, 3d and 4th amino acid groups in the presence of 5% glucose, whereas amino acids of the first group stimulate the protease synthesis in the presence of 2% glucose. The stimulatory effect of amino acids of the first groups is due to histidine and arginine.
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PMID:[Regulation of alkaline protease synthesis in Bacillus subtilis A-50]. 81 33

Diethylpyrocarbonate (DEPC) inactivated the neutral zinc proteinase from Bacillus mesentericus strain 76/Bacillus subtilis (MCP 76) by ethoxycarbonylation completely. Exposure of the enzyme to DEPC together with the competitive inhibitor Z-L-phenylalanine prevented the loss of activity toward both peptide and protein substrates. Treatment with hydroxylamine restored the catalytic properties of the modified MCP 76 to that of the native enzyme. After chymotryptic digestion of ethoxycarbonylated MCP 76 in the presence and absence of Z-L-phenylalanine a single histidyl residue essential for the enzyme activity was isolated and identified as histidine 231.
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PMID:Modification of a zinc proteinase from Bacillus mesentericus strain 76 by diethylpyrocarbonate. 189 47

The Bacillus subtilis sacU locus consists of two genes, degS and degU, which positively regulate the synthesis of several extracellular enzymes including the neutral and alkaline proteases. Both the DegS and DegU proteins have been purified from overproducing Escherichia coli strains harboring degS or degU gene-carrying plasmids, and the following results were obtained. DegS was autophosphorylated in the presence of [gamma-32P]ATP, and transferred the phosphoryl group to DegU. The transfer reaction was rapid in contrast to the autophosphorylation reaction. The phosphoryl groups incorporated into DegS and DegU were released at their own specific rates, the latter being twice faster than the former. The linkage between DegS and the phosphoryl moiety was unstable at acidic pH, whereas reverse was the case for the linkage between DegU and its phosphoryl group, suggesting that His and Asp are involved in the formation of DegS-phosphate and DegU-phosphate, respectively. Deletion of degS resulted in the reduced expression of the exocellular alkaline protease gene, aprE. These results suggest that phosphorylation of DegS by its own kinase activity and subsequent transfer of the phosphoryl group to DegU play a role in the activation of the aprE gene.
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PMID:Isolation and phosphorylation of the Bacillus subtilis degS and degU gene products. 212 96

We have cloned and determined the nucleotide sequence of a cDNA fragment for the entire coding region of the alkaline protease (Alp) from a filamentous ascomycete Aspergillus oryzae. According to the deduced amino acid sequence, Alp has a putative prepro region of 121 amino acids preceding the mature region, which consists of 282 amino acids. A consensus sequence of a signal peptide consisting of 21 amino acids is found at the N-terminus of the prepro region. The primary structure of the mature region shares extensive homology (29%-44%) with those of subtilisin families, and the three residues (Asp 32, His 64 and Ser 221 in subtilisin BPN') composing the active site are preserved. The entire cDNA, coding for prepro Alp, when introduced into the yeast Saccharomyces cerevisiae, directed the secretion of enzymatically active Alp into the culture medium, with its N-terminus and specific activity identical to native Aspergillus Alp.
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PMID:A full length cDNA clone for the alkaline protease from Aspergillus oryzae: structural analysis and expression in Saccharomyces cerevisiae. 269 47

In our effort to identify the proteolytic specificity of various hemorrhagic toxins isolated from western diamondback rattlesnake venom, hemorrhagic toxin b was isolated in homogeneous form by previously published methods. Hemorrhagic toxin b hydrolyzed glucagon, producing six fragments. The proteolytic sites were identified as Thr(5)-Phe(6), Thr(10)-Ser(11), Asp(15)-Ser(16), Asp(21)-Phe(22) and Try(25)-Leu(26). When oxidized insulin B chain was used, proteolysis occurred at four sites: Asn(3)-Gln(4), His(10)-Leu(11), Tyr(16)-Leu(17) and Gly(23)-Phe(24). The proteolytic specificity of hemorrhagic toxin b is quite different from those of the nonvenom proteases such as thermomycolin, aspergillopeptidase c, alkaline protease from Aspergillus flavus, elastase, subtilisin and papain.
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PMID:Proteolytic specificity of hemorrhagic toxin b from Crotalus atrox (western diamondback rattlesnake) venom. 286 65

Using reversed-phase high-performance liquid chromatography (HPLC) it was possible to isolate 32P-labelled active-site regions of various proteins from the bacterial phosphoenolpyruvate-dependent phosphotransferase system. The purified peptides obtained by proteolytic cleavage with Lys-C protease and trypsin were sequenced by the gas phase method. The fragments derived from enzyme I (MW 70 000) of two streptococcal species show 100% homology. The analogous peptide of Staphylococcus aureus Enzyme I differs in the N-terminal region. A labelled peptide from the glucose-specific enzyme III protein of Escherichia coli obtained by cleavage with alkaline protease was isolated and sequenced. It could be fitted into the primary structure of this protein, which was derived from DNA sequence data. The active-site histidine residue of this protein is therefore localized at position 91. The HPLC separation method described is suitable for the isolation of peptides derived from active sites containing labile amino acid derivatives such as phosphohistidines.
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PMID:The bacterial phosphoenolpyruvate-dependent phosphotransferase system. Isolation of active site peptides by reversed-phase high-performance liquid chromatography and determination of their primary structure. 392 66

The production of alkaline protease, collagenase and histidine utilization (Hut) enzymes by Vibrio alginolyticus wild-type, hutH1 and hutU1 strains was investigated. Alkaline protease synthesis was stimulated by histidine and urocanic acid in the wild-type and hutU1 strains. The hutH1 mutant alkaline protease production was stimulated by urocanic acid and not by histidine. The Hut enzymes in the wild-type strain were coordinately induced by histidine. Urocanase and formimino-hydrolase were induced by histidine in the hutH1 mutant which lacked histidase and was not able to convert histidine to urocanic acid. Collagenase production in peptone medium was inhibited in the hut mutants. It is concluded that in V. alginolyticus urocanic acid regulates alkaline protease synthesis but that the Hut enzymes are induced by histidine. The involvement of the Hut genetic system in the regulation of alkaline protease and collagenase synthesis is discussed.
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PMID:Regulation of hut enzymes and intracellular protease activities in Vibrio alginolyticus hut mutants. 612 84

Vibrio alginolyticus synthesized an inducible extracellular collagenase in a peptone medium during the stationary growth phase. These cultures also possessed extracellular alkaline serine protease activity. The alkaline protease activity did not require a specific inducer and it was produced in tryptone or minimal media. The collagenase was not produced in either the tryptone or minimal media. The alkaline protease activity was sensitive to catabolite repression by a number of carbon sources, including glucose, and by amino acids and ammonium ions. Cyclic AMP, dibutyryl cyclic AMP and cyclic GMP did not relieve catabolite repression. Histidine and urocanic acid stimulated the production of alkaline protease activity in tryptone and minimal media. Other compounds associated with the histidine utilization (hut) pathway did not increase alkaline protease activity. Histidine reversed the repression of alkaline protease activity by glucose of (NH4)2SO4 in minimal medium. Histidine and the compounds associated with the hut pathway inhibited collagenase production.
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PMID:Regulation of extracellular alkaline protease activity by histidine in a collagenolytic Vibrio alginolyticus strain. 627 66

Enzyme-IIIglc is part of the glucose phosphotransferase system of Escherichia coli and Salmonella typhimurium and is phosphorylated by phosphoenolpyruvate in a reaction requiring enzyme I (phosphoenolpyruvate-protein phosphotransferase), and the histidine-containing phospho-carrier protein HPr. In this paper we report the isolation of IIIglc from E. coli and the characterization of the active center. Alkaline hydrolysis of [32P]P-IIIglc and chromatography of the hydrolysate suggested that the phosphoryl group is bound to a histidyl residue in P-IIIglc of S. typhimurium. Here we present 1H-NMR measurements of IIIglc and P-IIIglc from E. coli which further substantiate that the phosphoryl group in P-IIIglc is linked to the N-3 position of a histidyl residue. After phosphorylation of IIIglc with [32P]Phosphoenolpyruvate, enzyme I and HPr, the phosphorylated protein was cleaved with either alkaline protease from Streptomyces griseus or subtilisin from Bacillus subtilis. According to amino acid analysis both proteases produced the same peptide carrying the phosphoryl group. The amino acid sequence of this peptide was found to be Val-His-Phe-Gly-Ile-Asp. The lower electrophoretic mobility of P-IIIglc on dodecylsulfate/polyacrylamide gels and its stronger binding to the hydrophobic matrix of a reversed-phase column compared to unphosphorylated protein may indicate a structural change following phosphoenolpyruvate-dependent phosphorylation.
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PMID:Phosphoenolpyruvate-dependent phosphorylation site in enzyme IIIglc of the Escherichia coli phosphotransferase system. 638 26


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