Displaying publications 1 - 20 of 23 in total

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  1. Purification and N-terminal amino acid sequence of fructose-6-phosphate phosphoketolase from Bifidobacterium longum BB536
    Fandi KG, Ghazali HM, Yazid AM, Raha AR
    Lett Appl Microbiol, 2001 Apr;32(4):235-9.
    PMID: 11298932
    AIMS: The key enzyme in the fructose-6-phosphate shunt in bifidobacteria, Fructose-6-phosphate phosphoketolase (F6PPK; E.C. 4.1.2.22.), was purified to electrophoretic homogeneity for the first time from Bifidobacterium longum (BB536).

    METHODS AND RESULTS: A three-step procedure comprising acetone fractionation followed by fast protein liquid chromatography (FPLC) resulted in a 30-fold purification. The purified enzyme had a molecular mass of 300 +/- 5 kDa as determined by gel filtration. It is probably a tetramer containing two different subunits with molecular masses of 93 +/- 1 kDa and 59 +/- 0.5 kDa, as determined by SDS-PAGE.

    CONCLUSION: The deduced N-terminal amino acid sequences of the two subunits revealed no significant similarity between them and other proteins when compared to the data bases of EMBL and SWISS-PROT, indicating that this could be the first report on N-terminal amino acid sequence of F6PPK.

    SIGNIFICANCE AND IMPACT OF THE STUDY: The data from this study will be used to design oligonucleotide probe specific for bifidobacteria and to study the gene encoded F6PPK.

    Matched MeSH terms: Aldehyde-Lyases/genetics; Aldehyde-Lyases/isolation & purification*; Aldehyde-Lyases/chemistry
  2. Structural and functional characterisation of a cold-active yet heat-tolerant dehydroquinase from Glaciozyma antarctica PI12
    Jaafar NR, Mahadi NM, Mackeen MM, Illias RM, Murad AMA, Abu Bakar FD
    J Biotechnol, 2021 Mar 10;329:118-127.
    PMID: 33539893 DOI: 10.1016/j.jbiotec.2021.01.019
    Dehydroquinase or 3-dehydroquinate dehydratase (DHQD) reversibly cleaves 3-dehydroquinate to form 3-dehydroshikimate. Here, we describe the functional and structural features of a cold active type II 3-dehydroquinate dehydratase from the psychrophilic yeast, Glaciozyma antarctica PI12 (GaDHQD). Functional studies showed that the enzyme was active at low temperatures (10-30 °C), but displayed maximal activity at 40 °C. Yet the enzyme was stable over a wide range of temperatures (10-70 °C) and between pH 6.0-10.0 with an optimum pH of 8.0. Interestingly, the enzyme was highly thermo-tolerant, denaturing only at approximately 84 °C. Three-dimensional structure analyses showed that the G. antarctica dehydroquinase (GaDHQD) possesses psychrophilic features in comparison with its mesophilic and thermophilic counterparts such as higher numbers of non-polar residues on the surface, lower numbers of arginine and higher numbers of glycine-residues with lower numbers of hydrophobic interactions. On the other hand, GaDHQD shares some traits (i.e. total number of hydrogen bonds, number of proline residues and overall folding) with its mesophilic and thermophilic counterparts. Combined, these features contribute synergistically towards the enzyme's ability to function at both low and high temperatures.
    Matched MeSH terms: Hydro-Lyases
  3. Fulltext Genome wide comprehensive analysis and web resource development on cell wall degrading enzymes from phyto-parasitic nematodes
    Rai KM, Balasubramanian VK, Welker CM, Pang M, Hii MM, Mendu V
    BMC Plant Biol, 2015;15:187.
    PMID: 26232118 DOI: 10.1186/s12870-015-0576-4
    The plant cell wall serves as a primary barrier against pathogen invasion. The success of a plant pathogen largely depends on its ability to overcome this barrier. During the infection process, plant parasitic nematodes secrete cell wall degrading enzymes (CWDEs) apart from piercing with their stylet, a sharp and hard mouthpart used for successful infection. CWDEs typically consist of cellulases, hemicellulases, and pectinases, which help the nematode to infect and establish the feeding structure or form a cyst. The study of nematode cell wall degrading enzymes not only enhance our understanding of the interaction between nematodes and their host, but also provides information on a novel source of enzymes for their potential use in biomass based biofuel/bioproduct industries. Although there is comprehensive information available on genome wide analysis of CWDEs for bacteria, fungi, termites and plants, but no comprehensive information available for plant pathogenic nematodes. Herein we have performed a genome wide analysis of CWDEs from the genome sequenced phyto pathogenic nematode species and developed a comprehensive publicly available database.
    Matched MeSH terms: Polysaccharide-Lyases/genetics; Polysaccharide-Lyases/metabolism
  4. Fulltext Hyaluronatelyase production by Streptococcus pneumoniae isolated from patients and carriers
    Yusof HA, Desa M NM, Masri SN, Malina O, Jamal F
    Trop Biomed, 2015 Sep;32(3):413-8.
    PMID: 26695201 MyJurnal
    Hyaluronatelyase produced by various microorganisms are capable of degrading hyaluronic acid in connective tissues and initiating the spread of infection by opening an access for the pathogen into host tissues. The present study attempts to determine the distribution of hyaluronatelyase-producing Streptococcus pneumoniae among invasive, non invasive and carriage isolates, and correlate it with the clinical sources, year of isolation, colonial morphology and their serotypes. A total of 100 isolates from various clinical samples were selected and screened for hyaluronatelyase production and presence of the encoding SpnHyl gene. All isolates possessed SpnHyl gene. Ninety-six isolates including 34 carriage isolates were positive for production of hyaluronatelyase. Four hyaluronatelyase-negative isolates were from blood (2 isolates) and sputum (2 isolates). No significant association was detected among hyaluronatelyase production and bacterial characteristics except for colonial morphology (p = 0.040). High percentages of hyaluronatelyase production in these isolates suggest their possible role as human pathogens.
    Matched MeSH terms: Polysaccharide-Lyases/analysis*; Polysaccharide-Lyases/genetics
  5. Bioengineering of the Plant Culture of Capsicum frutescens with Vanillin Synthase Gene for the Production of Vanillin
    Chee MJ, Lycett GW, Khoo TJ, Chin CF
    Mol Biotechnol, 2017 Jan;59(1):1-8.
    PMID: 27826796 DOI: 10.1007/s12033-016-9986-2
    Production of vanillin by bioengineering has gained popularity due to consumer demand toward vanillin produced by biological systems. Natural vanillin from vanilla beans is very expensive to produce compared to its synthetic counterpart. Current bioengineering works mainly involve microbial biotechnology. Therefore, alternative means to the current approaches are constantly being explored. This work describes the use of vanillin synthase (VpVAN), to bioconvert ferulic acid to vanillin in a plant system. The VpVAN enzyme had been shown to directly convert ferulic acid and its glucoside into vanillin and its glucoside, respectively. As the ferulic acid precursor and vanillin were found to be the intermediates in the phenylpropanoid biosynthetic pathway of Capsicum species, this work serves as a proof-of-concept for vanillin production using Capsicum frutescens (C. frutescens or hot chili pepper). The cells of C. frutescens were genetically transformed with a codon optimized VpVAN gene via biolistics. Transformed explants were selected and regenerated into callus. Successful integration of the gene cassette into the plant genome was confirmed by polymerase chain reaction. High-performance liquid chromatography was used to quantify the phenolic compounds detected in the callus tissues. The vanillin content of transformed calli was 0.057% compared to 0.0003% in untransformed calli.
    Matched MeSH terms: Hydro-Lyases/genetics; Hydro-Lyases/metabolism*
  6. Fulltext Functional and Structural Studies of a Multidomain Alginate Lyase from Persicobacter sp. CCB-QB2
    Sim PF, Furusawa G, Teh AH
    Sci Rep, 2017 10 20;7(1):13656.
    PMID: 29057942 DOI: 10.1038/s41598-017-13288-1
    AlyQ from Persicobacter sp. CCB-QB2 is an alginate lyase with three domains - a carbohydrate-binding domain modestly resembling family 16 carbohydrate-binding module (CBM16), a family 32 CBM (CBM32) domain, and an alginate lyase domain belonging to polysaccharide lyase family 7 (PL7). Although AlyQ can also act on polyguluronate (poly-G) and polymannuronate (poly-M), it is most active on alginate. Studies with truncated AlyQ showed that the CBM32 domain did not contribute to enhancing AlyQ's activity under the assayed conditions. Nevertheless, it could bind to cleaved but not intact alginate, indicating that the CBM32 domain recognises alginate termini. The crystal structure containing both CBM32 and catalytic domains show that they do not interact with one another. The CBM32 domain contains a conserved Arg that may bind to the carboxyl group of alginate. The catalytic domain, meanwhile, shares a conserved substrate-binding groove, and the presence of two negatively charged Asp residues may dictate substrate specificity especially at subsite +1. As Persicobacter sp. CCB-QB2 was unable to utilise alginate, AlyQ may function to help the bacterium degrade cell walls more efficiently.
    Matched MeSH terms: Polysaccharide-Lyases/metabolism*; Polysaccharide-Lyases/chemistry
  7. Mutation spectrum of and founder effects affecting the PTS gene in East Asian populations
    Chiu YH, Chang YC, Chang YH, Niu DM, Yang YL, Ye J, et al.
    J Hum Genet, 2012 Feb;57(2):145-52.
    PMID: 22237589 DOI: 10.1038/jhg.2011.146
    The enzyme 6-pyruvoyl-tetrahydropterin synthase (PTPS, gene symbol: PTS) is involved in the second step of the de novo biosynthesis of tetrahydrobiopterin (BH4), which is a vital cofactor of nitric oxide synthases and three types of aromatic amino acid hydroxylases; the latter are important enzymes in the production of neurotransmitters. We conducted a study of PTS mutations in East Asia, including Taiwan, Mainland China, Japan, South Korea, the Philippines, Thailand and Malaysia. A total of 43 mutations were identified, comprising 22 previously reported mutations and 21 new discovered mutations. Among these, the c.155A>G, c.259C>T, c. 272A>G, c.286G>A and c.84-291A>G mutations were the most common PTS mutations in East Asia, while the c.58T>C and c.243G>A mutations were, respectively, specific to Filipinos and Japanese originating from Okinawa. Further studies demonstrated that each of the mutations listed above was in linkage disequilibrium to a specific allele of polymorphic microsatellite marker, D11S1347. These results suggest the presence of founder effects that have affected these frequent mutations in East Asia populations. In this context, D11S1347 should become one of the most reliable polymorphic markers for use in prenatal diagnosis among PTPS deficient families, especially where mutations are yet to be identified.
    Matched MeSH terms: Phosphorus-Oxygen Lyases/deficiency; Phosphorus-Oxygen Lyases/genetics*
  8. Fulltext PCR-based construction and transformation of CodY gene deletion construct in Streptococcus Pneumoniae
    Aisyah Mohamed Rehan, Mohammad Izwan Enche Othman, Nor Munirah Mohd Amin, Intan Azura Shahdan, Hanani Ahmad Yusof@Hanafi
    International Medical Journal Malaysia, 2017;16(11):7-7.
    MyJurnal
    Streptococcus pneumoniae (S. pneumoniae) is a gram-positive diplococci belonging to the genus Streptococcus and it is a well-studied pathogenic bacterium. Pneumococcal diseases such as otitis media, pneumonia, sepsis and meningitis caused by pathogenic strains of S. pneumoniae still brought significant mortality and morbidity worldwide. The pathogenicity of S. pneumoniae is exerted by various virulence factors and one of it is the enzyme hyaluronate lyase. Hyaluronate lyase plays a major role in
    the invasive capability of S. pneumoniae. Its mechanism of action and crystallographic
    structure have been determinedbut its regulatory mechanism is still poorly understood.
    Drawing connections between the nutritional behaviour and invasive property of S.
    pneumoniae, CodY regulator is hypothesized as a potential hyaluronate lyase regulator.
    This work was aimed to construct CodY deficient mutant of S. pneumoniae to form
    foundational work for the study of CodY regulatory effect on hyaluronate lyase.
    Matched MeSH terms: Polysaccharide-Lyases
  9. Complete genome of the potential thermozyme producer Anoxybacillus gonensis G2(T) isolated from the Gönen hot springs in Turkey
    Lim YL, Chan KG, Ee R, Belduz AO, Canakci S, Kahar UM, et al.
    J Biotechnol, 2015 Oct 20;212:65-6.
    PMID: 26297905 DOI: 10.1016/j.jbiotec.2015.08.007
    Anoxybacillus gonensis type strain G2(T) (=NCIMB 13,933(T) =NCCB 100040(T)) has been isolated from the Gönen hot springs in Turkey. This strain produces a number of well-studied, biotechnologically important enzymes, including xylose isomerase, carboxylesterase, and fructose-1,6-bisphosphate aldolase. In addition, this strain is an excellent candidate for the bioremediation of areas with heavy metal pollution. Here, we present a high-quality, annotated, complete genome of A. gonensis G2(T). Furthermore, this report provides insights into several novel enzymes of strain G2(T) and their potential industrial applications.
    Matched MeSH terms: Aldehyde-Lyases
  10. Fulltext Pseudogene product YqiG is important for pflB expression and biohydrogen production in Escherichia coli BW25113
    Zakaria MA, Mohd Yusoff MZ, Zakaria MR, Hassan MA, Wood TK, Maeda T
    3 Biotech, 2018 Oct;8(10):435.
    PMID: 30306004 DOI: 10.1007/s13205-018-1461-2
    Pseudogenes in the Escherichia coli genome are assumed to be non-functional. In this study, Keio collection BW25113∆yqiG and YqiG-producing strain (BW25113/pCA24N-YqiG) were used to evaluate the importance of pseudogene yqiG in hydrogen metabolism. Our results show pseudogene protein YqiG was identified as an essential protein in the production of biohydrogen from glucose. The mutant yqiG decreased biohydrogen production from 37 µmol mg-1 protein to 6 µmol mg-1 protein compared to the wild-type strain, and glucose consumption was reduced by 80%. Through transcriptional analysis, we found that the yqiG mutation represses pflB transcription tenfold; pflB encodes pyruvate-formate lyase, one of the key enzymes in the anaerobic metabolism of E. coli. Moreover, production of YqiG stimulated glycolysis and increased biohydrogen productivity 1.5-fold compared to that of the wild-type strain. Thus, YqiG is important for the central glycolysis reaction and is able to influence hydrogen metabolism activity in E. coli.
    Matched MeSH terms: Lyases
  11. Fulltext Variant GADL1 and response to lithium in bipolar I disorder
    Consortium on Lithium Genetics, Hou L, Heilbronner U, Rietschel M, Kato T, Kuo PH, et al.
    N Engl J Med, 2014 05 08;370(19):1857-9.
    PMID: 24806176 DOI: 10.1056/NEJMc1401817
    Matched MeSH terms: Carboxy-Lyases/genetics*
  12. Fulltext Screening method for detection of immediate amino acid decarboxylases--producing bacteria implicated in food poisoning
    Hussain H, Mohd Fuat AR, Vimala B, Ghazali HM
    Trop Biomed, 2011 Aug;28(2):351-61.
    PMID: 22041756
    Assessment of amino acid decarboxylase activity can be conducted using tubed broth or plated agar. In this study, the test was carried out in microtitre plates containing lysine, ornithine, arginine, tyrosine, tryptophan, phenylalanine or histidine as biogenic amine precursors. Møller decarboxylase base broth (MDB) with or without 1% of a known amino acid were added to wells of a 96 well-microtitre plate. The wells were inoculated with Escherichia coli, Klebsiella pneumoniae, Acinetobacter anitratus or Staphylococcus aureus to the final concentration of 6.0 x 10(7) cfu/ml and incubated at 35ºC. The absorbance of the culture broth was read at 570 nm at 0, 1.0, 2.0, 3.0, 4.0, 5.5, 6.5 and 7.5 hour. Comparison of means of A'(570) between 0 hour and a specified incubation time was determined statistically. Positive decarboxylase activities were detected in the media inoculated with E. coli and K. pneumoniae in less than 6 hours. The current method is suitable for immediate producers of amino acid decarboxylase enzymes. It costs less as it uses less amino acid and it has the potential to be used for screening aliquots of food materials for amino acid decarboxylase activities.
    Matched MeSH terms: Carboxy-Lyases/metabolism*
  13. Red cell glyoxalase I and placental soluble aconitase polymorphisms in the three major ethnic groups of Malaysia
    Teng YS, Tan SG, Ng T, Lopez CG
    Jinrui Idengaku Zasshi, 1978 Sep;23(3):211-5.
    PMID: 732016
    Matched MeSH terms: Lyases/genetics*
  14. The draft genome of tropical fruit durian (Durio zibethinus)
    Teh BT, Lim K, Yong CH, Ng CCY, Rao SR, Rajasegaran V, et al.
    Nat Genet, 2017 Nov;49(11):1633-1641.
    PMID: 28991254 DOI: 10.1038/ng.3972
    Durian (Durio zibethinus) is a Southeast Asian tropical plant known for its hefty, spine-covered fruit and sulfury and onion-like odor. Here we present a draft genome assembly of D. zibethinus, representing the third plant genus in the Malvales order and first in the Helicteroideae subfamily to be sequenced. Single-molecule sequencing and chromosome contact maps enabled assembly of the highly heterozygous durian genome at chromosome-scale resolution. Transcriptomic analysis showed upregulation of sulfur-, ethylene-, and lipid-related pathways in durian fruits. We observed paleopolyploidization events shared by durian and cotton and durian-specific gene expansions in MGL (methionine γ-lyase), associated with production of volatile sulfur compounds (VSCs). MGL and the ethylene-related gene ACS (aminocyclopropane-1-carboxylic acid synthase) were upregulated in fruits concomitantly with their downstream metabolites (VSCs and ethylene), suggesting a potential association between ethylene biosynthesis and methionine regeneration via the Yang cycle. The durian genome provides a resource for tropical fruit biology and agronomy.
    Matched MeSH terms: Carbon-Sulfur Lyases/genetics*; Carbon-Sulfur Lyases/metabolism
  15. Fulltext Anti-snake venom and methanolic extract of Andrographis paniculata: a multipronged strategy to neutralize Naja naja venom acetylcholinesterase and hyaluronidase
    Nayak AG, Kumar N, Shenoy S, Roche M
    3 Biotech, 2020 Nov;10(11):476.
    PMID: 33083200 DOI: 10.1007/s13205-020-02462-4
    The study investigates the ability of methanolic extract of Andrographis paniculata (MAP) to supplement polyvalent anti-snake venom (ASV) in inhibiting neurotoxic enzyme acetylcholinesterase (AChE) and 'spreading factor' hyaluronidase from Naja naja (N.N) venom. AChE and hyaluronidase activity were measured in 100 or 200 µg of crude venom, respectively, and designated as 'control'. In Test Group I, enzyme assays were performed immediately after the addition of ASV/MAP/ASV + MAP to the venom. Inhibition of AChE by ASV (100-367 µg) was 12-17%, and of hyaluronidase (22-660 µg) was 33-41%. Under the same conditions, MAP (100-400 µg) inhibited AChE and hyaluronidase to the extent of 17-33% and 17-52%, respectively. When ASV (220 µg) and MAP (100-200 µg) were added together, AChE and hyaluronidase were inhibited to a greater extent from 39-63 to 36-44%, than when either of them was used alone. In Test Group 2, the venom was incubated with ASV/MAP/ASV + MAP for 10-30 min at 37 °C prior to the assay which enhanced AChE inhibition by 6%, 82% and 18% respectively, when compared to Test Group I. Though there was no change in inhibition of hyaluronidase in the presence of ASV, MAP could further increase the extent of inhibition by 27% and ASV + MAP upto 4%. In Test Group III, venom and substrate were incubated for 90 min and hyaluronidase activity was measured after the addition of inhibitors. Here, ASV + MAP caused increased inhibition by 69% compared to ASV alone. The study confirms the ability of phytochemicals in MAP to contribute to a multipronged strategy by supplementing, thereby augmenting the efficacy of ASV.
    Matched MeSH terms: Polysaccharide-Lyases
  16. Structural basis for binding uronic acids by family 32 carbohydrate-binding modules
    Teh AH, Sim PF, Hisano T
    Biochem Biophys Res Commun, 2020 12 10;533(3):257-261.
    PMID: 33010888 DOI: 10.1016/j.bbrc.2020.09.064
    The alginate lyase AlyQ from Persicobacter sp. CCB-QB2 is a three-domained enzyme with a carbohydrate-binding module (CBM) from family 32. The CBM32 domain, AlyQB, binds enzymatically cleaved but not intact alginate. Co-crystallisation of AlyQB with the cleaved alginate reveals that it binds to the 4,5-unsaturated mannuronic acid of the non-reducing end. The binding pocket contains a conserved R248 that interacts with the sugar's carboxyl group, as well as an invariant W303 that stacks against the unsaturated pyranose ring. Targeting specifically the non-reducing end is more efficient than the reducing end since the latter consists of a mixture of mannuronic acid and guluronic acid. AlyQB also seems unable to bind these two saturated sugars as they contain OH groups that will clash with the pocket. Docking analysis of YeCBM32, which binds oligogalacturonic acid, shows that the stacking of the pyranose ring is shifted in order to accommodate the sugar's axial C1-OH, and its R69 is accordingly elevated to bind the sugar's carboxyl group. Unlike AlyQB, YeCBM32's binding pocket is able to accommodate both saturated and unsaturated galacturonic acid.
    Matched MeSH terms: Polysaccharide-Lyases/genetics; Polysaccharide-Lyases/metabolism; Polysaccharide-Lyases/chemistry*
  17. Molecular dynamics simulations suggest changes in electrostatic interactions as a potential mechanism through which serine phosphorylation inhibits DNA Polymerase β's activity
    Homouz D, Joyce-Tan KH, Shahir Shamsir M, Moustafa IM, Idriss H
    J Mol Graph Model, 2018 01;79:192.
    PMID: 29223917 DOI: 10.1016/j.jmgm.2017.11.002
    DNA polymerase β is a 39kDa enzyme that is a major component of Base Excision Repair in human cells. The enzyme comprises two major domains, a 31kDa domain responsible for the polymerase activity and an 8kDa domain, which bind ssDNA and has a deoxyribose phosphate (dRP) lyase activity. DNA polymerase β was shown to be phosphorylated in vitro with protein kinase C (PKC) at serines 44 and 55 (S44 and S55), resulting in loss of its polymerase enzymic activity, but not its ability to bind ssDNA. In this study, we investigate the potential phosphorylation-induced structural changes for DNA polymerase β using molecular dynamics. The simulations show drastic conformational changes of the polymerase structure as a result of S44 phosphorylation. Phosphorylation-induced conformational changes transform the closed (active) enzyme structure into an open one. Further analysis of the results points to a key hydrogen bond and newly formed salt bridges as potential drivers of these structural fluctuations. The changes observed with S44/55 and S55 phosphorylation were less dramatic than S44 and the integrity of the H-bond was not compromised. Thus the phosphorylation of S44 is likely the major contributor to structural fluctuations that lead to loss of enzymatic activity.
    Matched MeSH terms: Lyases
  18. Cyanide degradation by pseudomonas pseudoalcaligenes strain W2 Isolated from mining effluent
    Belinda Tiong, Zaratulnur Mohd Bahari, Nor Sahslin Irwan Shah Lee, Zaharah Ibrahim, Shafinaz Shahir
    Sains Malaysiana, 2015;44:233-238.
    Cyanide is highly toxic to the living organisms as it inhibits respiration system in the cell mitochondria. Cyanide is commonly used in gold extraction process and its discharge into the environment not only causes pollution but it also brings harm to the surrounding population. Chemical treatment is expensive and the use of hazardous compound can exacerbate the problem. Biodegradation offers cheap and safe alternative as it overcomes the problems faced by chemical treatment. In this study, indigenous bacteria from mining wastewater were isolated. Cyanide degradation was done via shake flask method. A bacterium, designated W2 was found able to grow in the mining wastewater. 16S rRNA analysis identified the strain as Pseudomonas pseudoalcaligenes which could tolerate up to 39 mg/L cyanide concentration and growth was depleted at 52 mg/L. 60% cyanide degradation was achieved in wastewater containing medium. End-product analysis from high performance liquid chromatography (HPLC) detected formamide implicating the role of cyanide hydratase in cyanide degradation. It can be concluded that P. pseudoalcaligenes is capable of biodegrading cyanide and its potential in wastewater treatment containing cyanide is feasible.
    Matched MeSH terms: Hydro-Lyases
  19. Arabidopsis at2g02870 loss of function mutants lead to enhanced production of hydroperoxide lyase pathway genes and products
    Muhammad Naeem-ul-Hassan, Zamri Zainal, Ismanizan Ismail, Nur Athirah Abd Hamid, Muhammad Sajad
    Sains Malaysiana, 2018;47:3003-3008.
    F-box proteins containing variable C-terminal domains make an essential part of SKP1-Cullin-Ring box-F box (SCF)
    complex. SCF complex catalyzes the final step to link the ubiquitin tag with the target protein, destined for degradation,
    through F-box protein that confer overall substrate specificity to the complex. In this study, we analyzed the role of
    At2g02870, a Kelch containing F-box protein from Arabidopsis thaliana, by using reverse genetics strategy. At2g02870
    loss of function mutant lines (at2g02870) were analyzed and compared with wild type plants for the expression of genes
    and products of hydroperoxide lyase (HPL) branch of oxylipin pathway. We found that the at2g02870 plants have enhanced
    expression of HPL pathway genes and produce more green leaf volatiles (GLV) than the wild type plants. Our results
    suggested that the gene is involved in the regulation of HPL pathway, possibly through the degradation of enzymes or/
    and the regulatory factors of the pathway.
    Matched MeSH terms: Aldehyde-Lyases
  20. Crystal structure of fuculose aldolase from the Antarctic psychrophilic yeast Glaciozyma antarctica PI12
    Jaafar NR, Littler D, Beddoe T, Rossjohn J, Illias RM, Mahadi NM, et al.
    Acta Crystallogr F Struct Biol Commun, 2016 11 01;72(Pt 11):831-839.
    PMID: 27827354
    Fuculose-1-phosphate aldolase (FucA) catalyses the reversible cleavage of L-fuculose 1-phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde. This enzyme from mesophiles and thermophiles has been extensively studied; however, there is no report on this enzyme from a psychrophile. In this study, the gene encoding FucA from Glaciozyma antarctica PI12 (GaFucA) was cloned and the enzyme was overexpressed in Escherichia coli, purified and crystallized. The tetrameric structure of GaFucA was determined to 1.34 Å resolution. The overall architecture of GaFucA and its catalytically essential histidine triad are highly conserved among other fuculose aldolases. Comparisons of structural features between GaFucA and its mesophilic and thermophilic homologues revealed that the enzyme has typical psychrophilic attributes, indicated by the presence of a high number of nonpolar residues at the surface and a lower number of arginine residues.
    Matched MeSH terms: Aldehyde-Lyases/genetics; Aldehyde-Lyases/metabolism; Aldehyde-Lyases/chemistry*
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