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Lyase Activity (lyase + activity)
Selected AbstractsAntiinflammatory and Antihyaluronate Lyase Activities of Lanostanoids from Piptoporus betulinus.CHEMINFORM, Issue 21 2005Hilaire V. Kemami Wangun Abstract For Abstract see ChemInform Abstract in Full Text. [source] Completing the hypusine pathway in PlasmodiumFEBS JOURNAL, Issue 20 2009Deoxyhypusine hydroxylase is an E-Z type HEAT repeat protein In searching for new targets for antimalarials we investigated the biosynthesis of hypusine present in eukaryotic initiation factor-5A (eIF-5A) in Plasmodium. Here, we describe the cloning and expression of deoxyhypusine hydroxylase (DOHH), which completes the modification of eIF-5A through hydroxylation of deoxyhypusine. The dohh cDNA sequence revealed an ORF of 1236 bp encoding a protein of 412 amino acids with a calculated molecular mass of 46.45 kDa and an isoelectric point of 4.96. Interestingly, DOHH from Plasmodium has a FASTA SCORE of only 27 compared with its human ortholog and contains several matches similar to E-Z-type HEAT-like repeat proteins (IPR004155 (InterPro), PF03130 (Pfam), SM00567 (SMART) present in the phycocyanin lyase subunits of cyanobacteria. Purified DOHH protein displayed hydroxylase activity in a novel in vitro DOHH assay, but phycocyanin lyase activity was absent. dohh is present as a single-copy gene and is transcribed in the asexual blood stages of the parasite. A signal peptide at the N-terminus might direct the protein to a different cellular compartment. During evolution, Plasmodium falciparum acquired an apicoplast that lost its photosynthetic function. It is possible that plasmodial DOHH arose from an E/F-type phycobilin lyase that gained a new role in hydroxylation. Structured digital abstract ,,MINT-7255047: DHS (uniprotkb:P49366) enzymaticly reacts (MI:0414) with eIF-5A (uniprotkb:Q710D1) by enzymatic studies (MI:0415) ,,MINT-7255326: DOHH (uniprotkb:Q8I701) enzymaticly reacts (MI:0414) with eIF-5A (uniprotkb:Q710D1) by enzymatic studies (MI:0415) [source] Reassessment of treatments to retard browning of fresh-cut Russet potato with emphasis on controlled atmospheres and low concentrations of bisulphiteINTERNATIONAL JOURNAL OF FOOD SCIENCE & TECHNOLOGY, Issue 7 2010Yurong Ma Summary The cultivar Pacific Russet with high browning susceptibility was used for most testing. Controlled atmospheres (0.3%, 3% and 21% O2 in combination with 0%, 6% or 12% CO2) and anti-browning chemicals were studied in relation to quality retention and wound-induced phenolic metabolism of fresh-cut slices for up to 16 days at 5 °C. The 3% O2+ 12% CO2 atmosphere was most effective among those tested, and retarded increases in phenolics and phenylalanine ammonia lyase activity, but had only slight benefit on visual quality. A 1.25% ascorbic acid +1.25% citric acid treatment was ineffective, but when combined with 3% O2+ 12% CO2, it was comparable with 0.025% sodium bisulphite. Bisulphite concentrations from 0.05% to 0.25% provided similar effective control of discolouration. Bisulphite as low as 0.025% with 3% O2+ 12% CO2 resulted in a visual quality score at the limit of marketability after 8 days at 5 °C. Chemical treatments did not retard increases in phenolic concentrations or phenolic enzyme activities. [source] Stability of hydroperoxide lyase activity from Amaranthus tricolor (Amaranthus mangostanus L.) leaves: influence of selected additivesJOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, Issue 5 2010Zhen Long Abstract BACKGROUND: Hydroperoxide lyase (HPL) has potential value for the flavour additive industry. Currently, the production and application of HPL suffer from stability problems. The objective of this study was to investigate the stabilisation of HPL preparation from Amaranthus tricolor leaves by the addition of selected chemical additives. RESULTS:Amaranthus tricolor leaves were identified as a particularly rich source of 13-HPL activity. The addition of 100 g L,1 sucrose and trehalose to microsomal HPL prior to lyophilisation could retain nearly 100% enzymatic activity, compared to only 20% for the lyophilised control. The lyophilised microsomal HPL containing sucrose maintained full activity for even 40 days storage at , 20 °C. For HPL solution, glycerol was effective for long-term stability at , 20 °C. Moreover, poyols (sucrose and trehalose) and amino acid (glycine) enhanced the thermostability of HPL, while KCl and polyol mannitol decreased the thermostability of HPL. CONCLUSION: The flavour-producing enzyme HPL, found in the leaves of Amaranthus tricolor, was stabilised by the addition of chemical additives. Copyright © 2010 Society of Chemical Industry [source] Folate synthesis in plants: the last step of the p -aminobenzoate branch is catalyzed by a plastidial aminodeoxychorismate lyaseTHE PLANT JOURNAL, Issue 4 2004Gilles J.C. Basset Summary In plants, the last step in the synthesis of p -aminobenzoate (PABA) moiety of folate remains to be elucidated. In Escherichia coli, this step is catalyzed by the PabC protein, a , -lyase that converts 4-amino-4-deoxychorismate (ADC) , the reaction product of the PabA and PabB enzymes , to PABA and pyruvate. So far, the only known plant enzyme involved in PABA synthesis is ADC synthase, which has fused domains homologous to E. coli PabA and PabB and is located in plastids. ADC synthase has no lyase activity, implying that plants have a separate ADC lyase. No such lyase is known in any eukaryote. Genomic and phylogenetic approaches identified Arabidopsis and tomato cDNAs encoding PabC homologs with putative chloroplast-targeting peptides. These cDNAs were shown to encode functional enzymes by complementation of an E. coli pabC mutant, and by demonstrating that the partially purified recombinant proteins convert ADC to PABA. Plant ADC lyase is active as dimer and is not feedback inhibited by physiologic concentrations of PABA, its glucose ester, or folates. The full-length Arabidopsis ADC lyase polypeptide was translocated into isolated pea chloroplasts and, when fused to green fluorescent protein, directed the passenger protein to Arabidopsis chloroplasts in transient expression experiments. These data indicate that ADC lyase, like ADC synthase, is present in plastids. As shown previously for the ADC synthase transcript, the level of ADC lyase mRNA in the pericarp of tomato fruit falls sharply as ripening advances, suggesting that the expression of these two enzymes is coregulated. [source] Structure of putative 4-amino-4-deoxychorismate lyase from Thermus thermophilus HB8ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 12 2009Balasundaram Padmanabhan The pyridoxal 5,-phosphate-dependent enzyme 4-amino-4-deoxychorismate lyase converts 4-amino-4-deoxychorismate to p -aminobenzoate and pyruvate in one of the crucial steps in the folate-biosynthesis pathway. The primary structure of the hypothetical protein TTHA0621 from Thermus thermophilus HB8 suggests that TTHA0621 is a putative 4-amino-4-deoxychorismate lyase. Here, the crystal structure of TTHA0621 is reported at 1.93,Å resolution. The asymmetric unit contained four NCS molecules related by 222 noncrystallographic symmetry, in which the formation of intact dimers may be functionally important. The cofactor pyridoxal 5,-phosphate (PLP) binds to the protein in the large cleft formed by the N-terminal and C-terminal domains of TTHA0621. The high structural similarity and the conservation of the functional residues in the catalytic region compared with 4-amino-4-deoxychorismate lyase (PabC; EC 4.1.3.38) from Escherichia coli suggest that the TTHA0621 protein may also possess 4-amino-4-deoxychorismate lyase activity. [source] Inhibition of defective adenylosuccinate lyase by HNE: A neurological disease that may be affected by oxidative stressBIOFACTORS, Issue 1-4 2005C. Crifò Abstract Adenylosuccinate lyase is an enzyme of fumarase superfamily that participates in the purine biosynthetic pathway, catalysing the nonhydrolytic cleavage of succinyl groups from SAICA ribotide and adenylosuccinate. Enzyme defects are associated with a human inherited disease, which arises from single point mutations to the gene and results in mild to severe psychomotor retardation, epilepsy, muscle wasting, and autistic features. Adenylosuccinate lyase activity is lost to a different extent in the patients. Diminished levels of enzyme have been attributed to loss of catalytic activity, protein instability, or environmental factors. P100A/D422Y mutation represents a feasible model for studying the effect of cell milieu on the activity of the impaired enzyme. The defective enzyme is inhibited by micromolar concentrations of trans-4-hydroxy-2-nonenal (HNE), a major product of membrane peroxidation that has been found to accumulate in brain tissues of patients with neurodegenerative disorders. It is suggested that inactivation of defective adenylosuccinate lyase by HNE and other membrane peroxidation products may account, at least in part, for the impairment of neurological functions and recurrent worsening of the symptoms. [source] | |||||||||||||