Displaying publications 81 - 100 of 223 in total

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  1. Halmi, M.I.E.
    MyJurnal
    The rise in pollution cases globally is expected to increase in line with industrialization.
    Monitoring activities for pollutants have been hampered by the astronomical costs of
    instrumental-based approach. This has resulted in the intense research on low cost
    biomonitoring systems using enzymes, organisms including microorganisms. Only positive
    samples are sent for instrumental analysis; dramatically cutting the cost of instrumental
    analysis. This review attempts to outline and give due recognition to several selected bioassay
    systems that have been tested for their applicability using polluted water samples as a routine
    first line-of-defense. This includes small aquatic organisms-based assays, enzymes especially
    proteases and bacterial-based systems using respiratory dye or luminescence systems as a
    method for toxicant detection.
    Matched MeSH terms: Peptide Hydrolases
  2. Abdul Munir Abdul Murad, Rafidah Badrun, Sakina Shahabudin, Shazilah Kamaruddin, Madihah Ahmad Zairun, Farahayu Khairuddin, et al.
    Sains Malaysiana, 2013;42:715-724.
    Kitin merupakan polisakarida struktur yang dapat dicurai oleh enzim kitinolisis kepada pelbagai terbitan yang boleh digunakan dalam bidang perubatan, pertanian dan rawatan air. Pengenalpastian dan pencirian gen-gen Trichoderma virens UKM1 mengekod enzim terlibat dalam pencuraian kitin krustasea telah dilakukan melalui penjanaan penanda jujukan terekspres (ESTs) dan analisis pengekspresan gen menggunakan mikroatur DNA. Sebanyak tiga perpustakaan cDNA T. virens UKM1 yang masing-masing diaruh oleh kitin, glukosamina dan kitosan telah dibina. Sejumlah 1536 klon cDNA telah dijujuk dan sebanyak 1033 ESTs berkualiti telah dijana. Seterusnya, perbezaan pengekspresan gen apabila pertumbuhan kulat diaruh dengan kehadiran kitin krustasea dan tanpa kitin pada hari ketiga dan kelima telah ditentukan. Sebanyak 1824 klon cDNA telah dititik ke atas slaid kaca dan dihibrid bersama dengan cDNA terlabel Cy3 atau Cy5 yang disintesis daripada mRNA yang dipencil daripada kulat yang ditumbuhkan dalam medium mengandungi kitin krustasea atau glukosa (kawalan). Sebanyak 91 dan 61 gen, masing-masing bagi hari ketiga dan kelima didapati terekspres melebihi dua gandaan apabila kulat menggunakan kitin krustasea sebagai sumber karbon. Beberapa gen mengekod kitinase seperti ech1 dan cht3 (endokitinase), nag1 (eksokitinase) dan nagB (glukosamina 6-P-deaminase) didapati terekspres dengan tinggi pada kedua-dua hari. Selain daripada itu, gen mengekod protein hidrofobin, protease serina dan beberapa protein hipotetik juga terekspres dengan tinggi dengan kehadiran kitin krustasea. Protein-protein ini dijangka memainkan peranan penting dalam membantu pencuraian kitin krustasea.
    Matched MeSH terms: Peptide Hydrolases
  3. Le Van Thien, Ngo Thi Tuong Chau, Pham Thi Ngoc Lan, Hiroyuki Futamata
    Sains Malaysiana, 2018;47:1051-1060.
    Pulp and paper mill sludge (PPMS) was found to be poorly colonised with thermophilic microorganisms. However,
    evidence to support the need for inoculation to facilitate PPMS composting has only been demonstrated in one instance.
    In this study, we aimed to: screen and identify PPMS digesting thermophilic bacterial strains; investigate effects of the
    mixture of selected thermophilic bacterial strains on PPMS digestion; and utilize this mixture as start inoculum in PPMS
    composting and assess the quality of compost product. The results showed that eleven thermophilic bacterial strains were
    isolated from Bai Bang PPMS by the enrichment culture method. Among these, three strains which reflected high growth
    rates on the plates of Minimal Media Agar supplemented with Bai Bang PPMS and showed hydrolytic and ligninolytic
    activities on the agar plates containing appropriate inductive substrates were selected. Based on the morphological,
    biochemical characteristics and 16S rRNA gene sequencing, they were identified as Bacillus subtilis. The inoculation
    with the mixture of selected strains enhanced remarkably Bai Bang PPMS digestion. The dry weight decrease, volatile
    suspended solids removal, dehydrogenase and protease activities in the inoculated sludge were 2.1-, 1.5-, 1.3- and 1.2-
    fold higher, respectively, compared to the non-inoculated sludge. The assessment of compost quality based on stability
    using the alkaline trap method and maturity using the germination and root elongation test showed that the inoculated
    compost was stable and mature while the non-inoculated compost was unstable and immature. These thermophilic
    bacterial strains therefore have great potential for Bai Bang PPMS composting.
    Matched MeSH terms: Peptide Hydrolases
  4. Sayyed RZ, Wani SJ, Alarfaj AA, Syed A, El-Enshasy HA
    PLoS One, 2020;15(1):e0220095.
    PMID: 31910206 DOI: 10.1371/journal.pone.0220095
    There are numerous reports on poly-β-hydroxybutyrate (PHB) depolymerases produced by various microorganisms isolated from various habitats, however, reports on PHB depolymerase production by an isolate from plastic rich sites scares. Although PHB has attracted commercial significance, the inefficient production and recovery methods, inefficient purification of PHB depolymerase and lack of ample knowledge on PHB degradation by PHB depolymerase have hampered its large scale commercialization. Therefore, to ensure the biodegradability of biopolymers, it becomes imperative to study the purification of the biodegrading enzyme system. We report the production, purification, and characterization of extracellular PHB depolymerase from Stenotrophomonas sp. RZS7 isolated from a dumping yard rich in plastic waste. The isolate produced extracellular PHB depolymerase in the mineral salt medium (MSM) at 30°C during 4 days of incubation under shaking. The enzyme was purified by three methods namely ammonium salt precipitation, column chromatography, and solvent purification. Among these purification methods, the enzyme was best purified by column chromatography on the Octyl-Sepharose CL-4B column giving optimum yield (0.7993 Umg-1mL-1). The molecular weight of purified PHB depolymerase was 40 kDa. Studies on the assessment of biodegradation of PHB in liquid culture medium and under natural soil conditions confirmed PHB biodegradation potential of Stenotrophomonas sp. RZS7. The results obtained in Fourier-Transform Infrared (FTIR) analysis, High-Performance Liquid Chromatography (HPLC) study and Gas Chromatography Mass-Spectrometry (GC-MS) analysis confirmed the biodegradation of PHB in liquid medium by Stenotrophomonas sp. RZS7. Changes in surface morphology of PHB film in soil burial as observed in Field Emission Scanning Electron Microscopy (FESEM) analysis confirmed the biodegradation of PHB under natural soil environment. The isolate was capable of degrading PHB and it resulted in 87.74% biodegradation. A higher rate of degradation under the natural soil condition is the result of the activity of soil microbes that complemented the biodegradation of PHB by Stenotrophomonas sp. RZS7.
    Matched MeSH terms: Carboxylic Ester Hydrolases/biosynthesis; Carboxylic Ester Hydrolases/isolation & purification; Carboxylic Ester Hydrolases/chemistry*
  5. Mohamad Sobri MF, Abd-Aziz S, Abu Bakar FD, Ramli N
    Int J Mol Sci, 2020 Jun 04;21(11).
    PMID: 32512945 DOI: 10.3390/ijms21114035
    β-glucosidases (Bgl) are widely utilized for releasing non-reducing terminal glucosyl residues. Nevertheless, feedback inhibition by glucose end product has limited its application. A noticeable exception has been found for β-glucosidases of the glycoside hydrolase (GH) family 1, which exhibit tolerance and even stimulation by glucose. In this study, using local isolate Trichoderma asperellum UPM1, the gene encoding β-glucosidase from GH family 1, hereafter designated as TaBgl2, was isolated and characterized via in-silico analyses. A comparison of enzyme activity was subsequently made by heterologous expression in Escherichia coli BL21(DE3). The presence of N-terminal signature, cis-peptide bonds, conserved active site motifs, non-proline cis peptide bonds, substrate binding, and a lone conserved stabilizing tryptophan (W) residue confirms the identity of Trichoderma sp. GH family 1 β-glucosidase isolated. Glucose tolerance was suggested by the presence of 14 of 22 known consensus residues, along with corresponding residues L167 and P172, crucial in the retention of the active site's narrow cavity. Retention of 40% of relative hydrolytic activity on ρ-nitrophenyl-β-D-glucopyranoside (ρNPG) in a concentration of 0.2 M glucose was comparable to that of GH family 1 β-glucosidase (Cel1A) from Trichoderma reesei. This research thus underlines the potential in the prediction of enzymatic function, and of industrial importance, glucose tolerance of family 1 β-glucosidases following relevant in-silico analyses.
    Matched MeSH terms: Hydrolases
  6. Al-Nema MY, Gaurav A
    Curr Top Med Chem, 2020;20(26):2404-2421.
    PMID: 32533817 DOI: 10.2174/1568026620666200613202641
    Schizophrenia is a severe mental disorder that affects more than 1% of the population worldwide. Dopamine system dysfunction and alterations in glutamatergic neurotransmission are strongly implicated in the aetiology of schizophrenia. To date, antipsychotic drugs are the only available treatment for the symptoms of schizophrenia. These medications, which act as D2-receptor antagonist, adequately address the positive symptoms of the disease, but they fail to improve the negative symptoms and cognitive impairment. In schizophrenia, cognitive impairment is a core feature of the disorder. Therefore, the treatment of cognitive impairment and the other symptoms related to schizophrenia remains a significant unmet medical need. Currently, phosphodiesterases (PDEs) are considered the best drug target for the treatment of schizophrenia since many PDE subfamilies are abundant in the brain regions that are relevant to cognition. Thus, this review aims to illustrate the mechanism of PDEs in treating the symptoms of schizophrenia and summarises the encouraging results of PDE inhibitors as anti-schizophrenic drugs in preclinical and clinical studies.
    Matched MeSH terms: Phosphoric Diester Hydrolases
  7. Nur Zazarina Ramly, Nor Muhammad Mahadi, Noorul Aini Sulaiman
    Trop Life Sci Res, 2019;30(2):1-14.
    MyJurnal
    Pencirian enzim ekstraselular protease daripada bakteria Alkalophilic Bacillus lehensis G1 dari Malaysia telah dikaji. Enzim protease yang dirembeskan diuji pada agar susu skim 2%. Keputusan menunjukkan protease ekstraselular mampu mengekalkan aktiviti sehingga suhu 60°C di dalam julat pH yang luas iaitu 3 hingga 11 dengan suhu optimum pada 40°C dan pH optimum pada 7.0. Aktiviti enzim juga diperhatikan akan meningkat dengan penambahan beberapa ion iaitu Mn2+, Fe2+, Cu2+, Mg2+ dan Co2+. Manakala aktiviti protease didapati sedikit direncat dengan kehadiran ion Ca2+, K+ dan Ni2+ dengan baki aktiviti sebanyak 85%, 81% dan 75%. Protease ekstraselular juga didapati serasi dengan beberapa cecair detergen komersial dari Malaysia, yang menunjukkan protease ini boleh dimanfaatkan sebagai pembersih kotoran pada pakaian. Selain itu, potensi kegunaan protease yang dihasilkan oleh B. lehensis G1 ke atas penguraian gelatin dari filem X-ray yang telah digunakan juga telah dilakukan di dalam kajian ini.
    Matched MeSH terms: Peptide Hydrolases
  8. Tan NH, Armugam A, Tan CS
    Comp. Biochem. Physiol., B, 1989;93(4):757-62.
    PMID: 2553329
    1. The lethalities, anticoagulant effects, hermorrhagic, thrombin-like enzyme, hyaluronidase, protease, arginine ester hydrolase, 5'-nucleotidase, L-amino acid oxidase, alkaline phosphomonoesterase, phosphodiesterase and phospholipase A activities of twenty-three samples of venoms from twelve species of Asian lance-headed pit vipers (genus Trimeresurus) were examined. 2. The results indicate that notwithstanding individual variations in venom properties, the differences in biological properties of the Trimeresurus venoms can be used for the differentiation of venoms from different species of Trimeresurus. 3. The results also suggest that differences in the biological properties of snake venoms are useful parameters in the classification of snake species. 4. Our results indicate that venoms from the species T. okinavensis exhibited biological properties markedly different from other Trimeresurus venoms examined. This observation supports the recently proposed reclassification of T. okinavensis as a member of the genus Ovophis, rather than the genus Trimeresurus.
    Matched MeSH terms: Carboxylic Ester Hydrolases/metabolism; Phosphoric Diester Hydrolases/metabolism
  9. Ng, K.L., Mohd Khan, A.
    MyJurnal
    Utilization of palm kernel expeller (PKE), a palm oil milling by-product, may be diversified through the exploitation of its protein component. The PKE protein could be effectively extracted using an alkaline
    solution and followed by enzymatic hydrolysis to produce PKE protein hydrolysates or crude PKE peptide. The extraction of PKE protein was successfully carried out using an alkaline solution at pH11, at ratio of 1:10 (g/ml), PKE powder to alkaline solution with continuous shaking, 150 rpm, in a water bath operating at 50°C for 30 min. The extracted protein powder (PKEP) had 68.50±3.08% crude protein, 0.54±0.03% fat and 0.73±0.02% ash. The freeze-dried PKEP was re-suspend in particular buffer and hydrolyzed with proteolytic enzymes (Alcalase® 2.4L, Flavourzyme® 500MG, pepsin or trypsin) to obtain PKEP hydrolysate (PKEPH). The effect of enzyme concentration (0, 2, 4, 6, 8 & 10%) and time of hydrolysis (0, 6, 12, 24, 48 h) was studied to determine the most efficient hydrolytic conditions. Results showed that all enzymes tested were capable of hydrolyzing the PKEP and producing hydrolysates with different degree of hydrolysis (DH%). At 8.0% concentration, Alcalase®2.4L hydrolyzed PKEP into the highest DH (75.96%) hydrolysate (PKEPH) after 1h hydrolysis. Although only with 2.0% Alcalase 2.4 L concentration, it was sufficient to produce PKEP hydrolysate of 81.35% DH %, but it required 12 h to hydrolyze the protein. Pepsin was relatively the least efficient protease to hydrolyze the PKEP.
    Matched MeSH terms: Peptide Hydrolases
  10. Herpandi, Huda, N., Rosma, A., Wan Nadiah W. A.
    MyJurnal
    Protein-rich by-products from the canning industry, especially dark flesh of skipjack, have limited uses due to several factors such as darken color, susceptibility to oxidation and off flavour. Protein hydrolysates from skipjack dark flesh was produced with different type of industrial proteases (Alcalase®2.4L FG, Protamex®, Neutrase®1.5MG and Flavourzyme®500MG) for 60, 120, 180 and 240 min with level of proteases used of 0.5, 1, 1.5 and 2% per weight of raw material. The degree of hydrolysis and free tryptophan content of hydrolysate were investigated. The results shows longer time with higher concentration of enzyme has increased the degree of hydrolysis. Alcalase®2.4L FG had the highest degree of hydrolysis among all proteases followed by Protamex®, Flavourzyme®500MG and Neutrase® 1.5MG. All enzymes increase free tryptophan content linearly with the increament of protease enzyme level. The longer the hydrolysis time, the higher the content of free tryptophan produced.
    Matched MeSH terms: Peptide Hydrolases
  11. Seman WM, Bakar SA, Bukhari NA, Gaspar SM, Othman R, Nathan S, et al.
    J Biotechnol, 2014 Aug 20;184:219-28.
    PMID: 24910973 DOI: 10.1016/j.jbiotec.2014.05.034
    A Pichia pastoris transformant carrying the cutinase cDNA of Glomerella cingulata was over-expressed in a 5L bioreactor (2.0L working volume) under fed-batch conditions. Bioreactor experiments rely on varying selected parameters in repeated rounds of optimisation: here these included duration of induction, pH and temperature. Highest cell densities (320gL(-1) wet cell weight) with a cutinase production of 3800mgL(-1) and an activity of 434UmL(-1) were achieved 24h after induction with methanol in basal salt medium (at pH 5 and 28°C). Characterisation of the cutinase showed that it was stable between pH 6 and pH 11, had an optimum pH of 8.0 and retained activity for 30min at 50°C (optimum temperature 25°C).The preferred substrates of G. cingulata cutinase were the medium- to long-chain ρ-nitrophenyl esters of ρ-nitrophenylcaprylate (C8), ρ-nitrophenyllaurate (C12) and ρ-nitrophenylmyristate (C14), with the highest catalytic efficiency, kcat/Km of 7.7±0.7mM(-1)s(-1) for ρ-nitrophenylcaprylate. Microscopic analyses showed that the G. cingulata cutinase was also capable of depolymerising the high molecular weight synthetic polyester, polyethylene terephthalate.
    Matched MeSH terms: Carboxylic Ester Hydrolases/biosynthesis*; Carboxylic Ester Hydrolases/metabolism; Carboxylic Ester Hydrolases/chemistry
  12. Teo CY, Shave S, Chor AL, Salleh AB, Rahman MB, Walkinshaw MD, et al.
    BMC Bioinformatics, 2012;13 Suppl 17:S4.
    PMID: 23282142 DOI: 10.1186/1471-2105-13-S17-S4
    BACKGROUND: Rheumatoid arthritis (RA) is an autoimmune disease with unknown etiology. Anticitrullinated protein autoantibody has been documented as a highly specific autoantibody associated with RA. Protein arginine deiminase type 4 (PAD4) is the enzyme responsible for catalyzing the conversion of peptidylarginine into peptidylcitrulline. PAD4 is a new therapeutic target for RA treatment. In order to search for inhibitors of PAD4, structure-based virtual screening was performed using LIDAEUS (Ligand discovery at Edinburgh university). Potential inhibitors were screened experimentally by inhibition assays.

    RESULTS: Twenty two of the top-ranked water-soluble compounds were selected for inhibitory screening against PAD4. Three compounds showed significant inhibition of PAD4 and their IC50 values were investigated. The structures of the three compounds show no resemblance with previously discovered PAD4 inhibitors, nor with existing drugs for RA treatment.

    CONCLUSION: Three compounds were discovered as potential inhibitors of PAD4 by virtual screening. The compounds are commercially available and can be used as scaffolds to design more potent inhibitors against PAD4.

    Matched MeSH terms: Hydrolases/antagonists & inhibitors*; Hydrolases/biosynthesis; Hydrolases/chemistry
  13. Nishiki I, Minami T, Chen SC, Itami T, Yoshida T
    J Gen Appl Microbiol, 2012;58(6):457-63.
    PMID: 23337581
    Group C Streptococcus dysgalactiae (GCSD) is a pathogen of farmed fish. Almost all GCSD isolates from Asian countries, including Japan, Taiwan, Malaysia, and China, have a serum opacity factor (SOF-FD). Although the SOF-FD sequences in different GCSD isolates are identical, different opacification activities are observed. Three types of variations were observed in the upstream sequence of the sof-FD gene in GCSD isolates with different SOF-FD activities. Type 1 was characterized by insertion of an IS981-like element into the upstream region of the sof-FD gene. In Type 2, an IS981-like element was inserted into the upstream region in a direction opposite to that in Type 1. In Type 3, no IS element was inserted. Type 1 was predominant among Japanese isolates (129 of 133). Isolates from other Asian countries were generally Type 3 (13 of 16). Except for 1 strain, Type 1 strains exhibited opacification activities with optical densities (ODs)>0.6, while Type 2 and Type 3 strains have low opacification activities (ODs >0.2). Only Type 1 strains have putative -10 and -35 promoter regions upstream of the sof-FD gene, and the expression level of the sof-FD gene was higher in Type 1 strains than in Type 2 and Type 3 strains.
    Matched MeSH terms: Peptide Hydrolases/genetics; Peptide Hydrolases/metabolism*; Peptide Hydrolases/chemistry
  14. Nyon MP, Rice DW, Berrisford JM, Hounslow AM, Moir AJ, Huang H, et al.
    J Mol Biol, 2009 Jan 9;385(1):226-35.
    PMID: 18983850 DOI: 10.1016/j.jmb.2008.10.050
    Cutinase belongs to a group of enzymes that catalyze the hydrolysis of esters and triglycerides. Structural studies on the enzyme from Fusarium solani have revealed the presence of a classic catalytic triad that has been implicated in the enzyme's mechanism. We have solved the crystal structure of Glomerella cingulata cutinase in the absence and in the presence of the inhibitors E600 (diethyl p-nitrophenyl phosphate) and PETFP (3-phenethylthio-1,1,1-trifluoropropan-2-one) to resolutions between 2.6 and 1.9 A. Analysis of these structures reveals that the catalytic triad (Ser136, Asp191, and His204) adopts an unusual configuration with the putative essential histidine His204 swung out of the active site into a position where it is unable to participate in catalysis, with the imidazole ring 11 A away from its expected position. Solution-state NMR experiments are consistent with the disrupted configuration of the triad observed crystallographically. H204N, a site-directed mutant, was shown to be catalytically inactive, confirming the importance of this residue in the enzyme mechanism. These findings suggest that, during its catalytic cycle, cutinase undergoes a significant conformational rearrangement converting the loop bearing the histidine from an inactive conformation, in which the histidine of the triad is solvent exposed, to an active conformation, in which the triad assumes a classic configuration.
    Matched MeSH terms: Carboxylic Ester Hydrolases/antagonists & inhibitors; Carboxylic Ester Hydrolases/metabolism*; Carboxylic Ester Hydrolases/chemistry*
  15. Khan A, Shahab M, Nasir F, Waheed Y, Alshammari A, Mohammad A, et al.
    SAR QSAR Environ Res, 2023;34(9):689-708.
    PMID: 37675795 DOI: 10.1080/1062936X.2023.2250723
    In the current study, we used molecular screening and simulation approaches to target I7L protease from monkeypox virus (mpox) from the Traditional Chinese Medicines (TCM) database. Using molecular screening, only four hits TCM27763, TCM33057, TCM34450 and TCM31564 demonstrated better pharmacological potential than TTP6171 (control). Binding of these molecules targeted Trp168, Asn171, Arg196, Cys237, Ser240, Trp242, Glu325, Ser326, and Cys328 residues and may affect the function of I7L protease in in vitro assay. Moreover, molecular simulation revealed stable dynamics, tighter structural packing and less flexible behaviour for all the complexes. We further reported that the average hydrogen bonds in TCM27763, TCM33057, TCM34450 and TCM31564I7L complexes remained higher than the control drug. Finally, the BF energy results revealed -62.60 ± 0.65 for the controlI7L complex, for the TCM27763I7L complex -71.92 ± 0.70 kcal/mol, for the TCM33057I7L complex the BF energy was -70.94 ± 0.70 kcal/mol, for the TCM34450I7L the BF energy was -69.94 ± 0.85 kcal/mol while for the TCM31564I7L complex the BF energy was calculated to be -69.16 ± 0.80 kcal/mol. Although, we used stateoftheart computational methods, these are theoretical insights that need further experimental validation.
    Matched MeSH terms: Peptide Hydrolases
  16. Poli A, Nicolaus B, Chan KG, Kahar UM, Chan CS, Goh KM
    Genome Announc, 2015;3(3).
    PMID: 25999577 DOI: 10.1128/genomeA.00490-15
    Anoxybacillus thermarum AF/04(T) was isolated from the Euganean hot springs in Abano Terme, Italy. The present work reports a high-quality draft genome sequence of strain AF/04(T). This work also provides useful insights into glycoside hydrolases, glycoside transferases, and sugar transporters that may be involved in cellular carbohydrate metabolism.
    Matched MeSH terms: Glycoside Hydrolases
  17. Sudi IY, Shamsir MS, Jamaluddin H, Wahab RA, Huyop F
    Biotechnology, biotechnological equipment, 2014 Sep 03;28(5):949-957.
    PMID: 26019583
    The D-2-haloacid dehalogenase of D-specific dehalogenase (DehD) from Rhizobium sp. RC1 catalyses the hydrolytic dehalogenation of D-haloalkanoic acids, inverting the substrate-product configuration and thereby forming the corresponding L-hydroxyalkanoic acids. Our investigations were focused on DehD mutants: R134A and Y135A. We examined the possible interactions between these mutants with haloalkanoic acids and characterized the key catalytic residues in the wild-type dehalogenase, to design dehalogenase enzyme(s) with improved potential for dehalogenation of a wider range of substrates. Three natural substrates of wild-type DehD, specifically, monochloroacetate, monobromoacetate and D,L-2,3-dichloropropionate, and eight other non-natural haloalkanoic acids substrates of DehD, namely, L-2-chloropropionate; L-2-bromopropionate; 2,2-dichloropropionate; dichloroacetate; dibromoacetate; trichloroacetate; tribromoacetate; and 3-chloropropionate, were docked into the active site of the DehD mutants R134A and Y135A, which produced altered catalytic functions. The mutants interacted strongly with substrates that wild-type DehD does not interact with or degrade. The interaction was particularly enhanced with 3-chloropropionate, in addition to monobromoacetate, monochloroacetate and D,L-2,3-dichloropropionate. In summary, DehD variants R134A and Y135A demonstrated increased propensity for binding haloalkanoic acid and were non-stereospecific towards halogenated substrates. The improved characteristics in these mutants suggest that their functionality could be further exploited and harnessed in bioremediations and biotechnological applications.
    Matched MeSH terms: Hydrolases
  18. Ghassem M, Fern SS, Said M, Ali ZM, Ibrahim S, Babji AS
    J Food Sci Technol, 2014 Mar;51(3):467-75.
    PMID: 24587521 DOI: 10.1007/s13197-011-0526-6
    This study was conducted to evaluate the kinetic characteristics of proteolytic activity of proteases on Channa striatus protein fractions. Degree of hydrolysis (DH), amino acid composition and kinetic parameters of sarcoplasmic and myofibrillar proteins were investigated when incubated with proteinase K and thermolysin, separately. After 30 min incubation with proteases, a decrease in DH of sarcoplasmic protein was observed whereas, hydrolysis of myofibrillar protein with proteases took 2 h with an increase in DH. The major amino acids were glutamic acid (16.6%) in thermolysin- myofibrillar hydrolysate followed by aspartic acid (11.1%) in sarcoplasmic protein fraction with no enzyme treatment and lysine (10%) in thermolysin-myofibrillar hydrolysate. The apparent Michaelis constant of proteinase K was lower than thermolysin for both sarcoplasmic and myofibrillar proteins. However, rate of turnover and enzyme efficiency suggested that sarcoplasmic and myofibrillar proteins are suitable substrates for proteinase K and thermolysin hydrolytic reaction, respectively.
    Matched MeSH terms: Peptide Hydrolases
  19. Yew SM, Chan CL, Soo-Hoo TS, Na SL, Ong SS, Hassan H, et al.
    Genome Announc, 2013;1(3).
    PMID: 23723391 DOI: 10.1128/genomeA.00158-13
    Pyrenochaeta, classified under the order Pleosporales, is known to cause diseases in plants and humans. Here, we report a draft genome sequence of a Pyrenochaeta sp. isolated from a skin scraping, with an estimated genome size of 39.4 Mb. Genes associated with the synthesis of proteases, toxins, plant cell wall degradation, and multidrug resistance were found.
    Matched MeSH terms: Peptide Hydrolases
  20. Abdalsatar Abdalrazaq N, Ezleen Binti Kamarulzaman E
    Arch Razi Inst, 2022 Apr;77(2):843-852.
    PMID: 36284983 DOI: 10.22092/ARI.2022.357124.1980
    Nowadays dengue virus infection (DENV) is one of the major health complications in the world. Although DENV is an old and common disease, unfortunately, until now, there are no specific relevant treatments available for it. This study, therefore, aimed to design, as well as synthesize selective peptide inhibitors, and investigate their activity by in-vitro NS2B/NS3 protease inhibition assay. The design of the peptide ligands was based on studying the interactions with the dengue NS2B/NS3 protease using the computational docking technique in the MOE and AutoDock (version 4.2) software. To this end, the researchers designed 26 linear pentapeptides based on previous studies. It was revealed that two linear pentapeptides (i.e., GKRRK and KRRRK) are the best potential inhibitors. Furthermore, based on the findings of the two independent docking programs, the peptide GKRRK was synthesized by solid-phase peptide synthesis and its structure was confirmed. The in-vitro protease inhibitor study was conducted for these two peptides to examine their activity against the dengue virus using a protin in as a control. It was found that the designed potential peptides possess interesting inhibition against the NS2B/NS3 protease. Additionally, the findings showed that the peptide GKRRK had the highest percentage of inhibition (71.11%) at 100 µM with the IC50 of 48.87 µM; therefore, this linear peptide could serve as a good inhibitor for the DENV.
    Matched MeSH terms: Peptide Hydrolases
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