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Block Report for: H

Arylacetamide_deacetylase, BD-FAE, Est9X, GTSAGmotif, Hormone-sensitive_lipase_like, Kynurenine-formamidase, Plant_carboxylesterase, Steryl_acetyl_hydrolase, Tannase_Bact

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FamilyArylacetamide_deacetylase
CommentAADAC Arylacetamide deacetylase displays cellular triglyceride lipase activity in liver, increases the levels of intracellular fatty acids derived from the hydrolysis of newly formed triglyceride stores and plays a role in very low-density lipoprotein assembly. Displays serine esterase activity in liver. Deacetylates a variety of arylacetamide substrates, including xenobiotic compounds and procarcinogens, converting them to the primary arylamide compounds and increasing their toxicity. NCEH1 KIAA1363 AADACL1 NCEH1 neutral cholesterol ester hydrolase 1.is highly expressed in invasive cancer cells and is the major protein in mouse brain diethylphosphorylated . Sequence similarities between hormone-sensitive lipase and prokaryotic enzymes was dicovered by Langin and Holm and Hemila et al.
InterproIPR017157 (Arylacetamide deacetylase), IPR013094 (Alpha/beta hydrolase fold-3)Pdoc
PFamPF07859 (Abhydrolase_3)PrintsProsite
EC no EC numberTables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
    Title: Impact of AADAC gene expression on prognosis in patients with Borrmann type III advanced gastric cancer
    Wang Y, Fang T, Yin X, Zhang L, Zhang X, Zhang D, Zhang Y, Wang X, Wang H, Xue Y
    Ref: BMC Cancer, 22:635, 2022 : PubMed

            

    Title: Arylacetamide Deacetylase Is Involved in Vicagrel Bioactivation in Humans
    Jiang J, Chen X, Zhong D
    Ref: Front Pharmacol, 8:846, 2017 : PubMed

            

    Title: Comparison of substrate specificity among human arylacetamide deacetylase and carboxylesterases
    Fukami T, Kariya M, Kurokawa T, Iida A, Nakajima M
    Ref: Eur J Pharm Sci, 78:47, 2015 : PubMed

            

    Title: Dual roles of brain serine hydrolase KIAA1363 in ether lipid metabolism and organophosphate detoxification
    Nomura DK, Fujioka K, Issa RS, Ward AM, Cravatt BF, Casida JE
    Ref: Toxicol Appl Pharmacol, 228:42, 2008 : PubMed

            

    Title: Synthesis and function of hepatic very-low-density lipoprotein
    Gibbons GF, Wiggins D, Brown AM, Hebbachi AM
    Ref: Biochemical Society Transactions, 32:59, 2004 : PubMed

            

    Title: Human liver arylacetamide deacetylase: Molecular cloning of a novel esterase involved in the metabolic activation of arylamine carcinogens with high sequence similarity to hormone sensitive lipase
    Probst MR, Beer M, Beer D, Jenoe P, Meyer UA, Gasser R
    Ref: Journal of Biological Chemistry, 34:21650, 1994 : PubMed

            

> Structure scheme for Arylacetamide_deacetylase
no Structure
> List of Gene_Locus for Arylacetamide_deacetylase (454)


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FamilyBD-FAE
CommentExtracted from Hormone sensitive lipases. BD-FAE: The function of many members may differ from the one of the representavive used to describe the family in the PFAM database. (from PFAM): This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilisation loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates. In PFAM database it includes family Tannase_Bact and family Est9X which are separate families in ESTHER
InterproPdoc
PFamPF20434 (BD-FAE)PrintsProsite
EC no EC numberTables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
    Title: A Thermophilic Bacterial Esterase for Scavenging Nerve Agents: A Kinetic, Biophysical and Structural Study
    Bzdrenga J, Trenet E, Chantegreil F, Bernal K, Nachon F, Brazzolotto X
    Ref: Molecules, 26:657, 2021 : PubMed

            

    Title: Polysaccharide utilization loci-driven enzyme discovery reveals BD-FAE: a bifunctional feruloyl and acetyl xylan esterase active on complex natural xylans
    Hameleers L, Penttinen L, Ikonen M, Jaillot L, Faure R, Terrapon N, Deuss PJ, Hakulinen N, Master ER, Jurak E
    Ref: Biotechnol Biofuels, 14:127, 2021 : PubMed

            

    Title: Structural Insights into the Dual-Substrate Recognition and Catalytic Mechanisms of a Bifunctional Acetyl Ester-Xyloside Hydrolase from Caldicellulosiruptor lactoaceticus
    Cao H, Sun L, Huang Y, Liu X, Yang D, Liu T, Jia X, Wen B, Gu T and Xin F <1 more author(s)>
    Ref: ACS Catal, 9:1739, 2019 : PubMed

            

    Title: Pressure adaptation is linked to thermal adaptation in salt-saturated marine habitats
    Alcaide M, Stogios PJ, Lafraya A, Tchigvintsev A, Flick R, Bargiela R, Chernikova TN, Reva ON, Hai T and Ferrer M <11 more author(s)>
    Ref: Environ Microbiol, 17:332, 2015 : PubMed

            

    Title: A Lactobacillus plantarum Esterase Active on a Broad Range of Phenolic Esters
    Esteban-Torres M, Landete JM, Reveron I, Santamaria L, de Las Rivas B, Munoz R
    Ref: Applied Environmental Microbiology, 81:3235, 2015 : PubMed

            

    Title: The Structure of a Novel Thermophilic Esterase from the Planctomycetes Species, Reveals an Open Active Site Due to a Minimal 'Cap' Domain
    Sayer C, Szabo Z, Isupov MN, Ingham C, Littlechild JA
    Ref: Front Microbiol, 6:1294, 2015 : PubMed

            

    Title: Structure, biochemical characterization and analysis of the pleomorphism of carboxylesterase Cest-2923 from Lactobacillus plantarum WCFS1
    Benavente R, Esteban-Torres M, Acebron I, de Las Rivas B, Munoz R, Alvarez Y, Mancheno JM
    Ref: Febs J, 280:6658, 2013 : PubMed

            

no Image
&gt; Structures for BD-FAE (27)
&gt; List of Gene_Locus for BD-FAE (775)


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FamilyEst9X
CommentBacterial esterases. Fang et al. described a novel esterase from a marine metagenomic library exhibiting high salt tolerance. The enzyme is essentially active on pNP-C2 C4 and C6. The family is extracted from 6_AlphaBeta_hydrolase. This family differs from all the families of the Arpigny Jaeger classification.
InterproPdoc
PFamPrintsProsite
EC no EC numberTables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
    Title: Characterization of a novel hyper-thermostable and chlorpyrifos-hydrolyzing carboxylesterase EstC: A representative of the new esterase family XIX
    Wang B, Wu S, Chang X, Chen J, Ma J, Wang P, Zhu G
    Ref: Pestic Biochem Physiol, 170:104704, 2020 : PubMed

            

    Title: A novel esterase from a marine metagenomic library exhibiting salt tolerance ability
    Fang Z, Li J, Wang Q, Fang W, Peng H, Zhang X, Xiao Y
    Ref: J Microbiol Biotechnol, 24:771, 2014 : PubMed

            

no Image
no Structure
&gt; List of Gene_Locus for Est9X (169)


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FamilyGTSAGmotif
CommentSequences of lipases from metagenomic library were grouped in a new subset of Alphabeta hydrolase fold-3 (Arpigny_Jaeger Family_IV). Most sequences have a G(TDC)SA(G)G motif encompassing the active site serine.
InterproIPR013094 (Alpha/beta hydrolase fold-3)Pdoc
PFamPF07859 (Abhydrolase_3)PrintsProsite
EC no EC numberTables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
    Title: Crystal structure of PMGL2 esterase from the hormone-sensitive lipase family with GCSAG motif around the catalytic serine
    Boyko KM, Kryukova MV, Petrovskaya LE, Nikolaeva AY, Korzhenevsky DA, Novototskaya-Vlasova KA, Rivkina EM, Dolgikh DA, Kirpichnikov MP, Popov VO
    Ref: PLoS ONE, 15:e0226838, 2020 : PubMed

            

    Title: Expression and characterization of a new esterase with GCSAG motif from a permafrost metagenomic library
    Petrovskaya LE, Novototskaya-Vlasova KA, Spirina EV, Durdenko EV, Lomakina GY, Zavialova MG, Nikolaev EN, Rivkina EM
    Ref: FEMS Microbiol Ecol, 92:, 2016 : PubMed

            

    Title: Pressure adaptation is linked to thermal adaptation in salt-saturated marine habitats
    Alcaide M, Stogios PJ, Lafraya A, Tchigvintsev A, Flick R, Bargiela R, Chernikova TN, Reva ON, Hai T and Ferrer M <11 more author(s)>
    Ref: Environ Microbiol, 17:332, 2015 : PubMed

            

    Title: Structural Basis for Dimerization and Catalysis of a Novel Esterase from the GTSAG Motif Subfamily of the Bacterial Hormone-sensitive Lipase Family
    Li PY, Ji P, Li CY, Zhang Y, Wang GL, Zhang XY, Xie BB, Qin QL, Chen XL and Zhang YZ <1 more author(s)>
    Ref: Journal of Biological Chemistry, 289:19031, 2014 : PubMed

            

    Title: Identification of a new subfamily of salt-tolerant esterases from a metagenomic library of tidal flat sediment
    Jeon JH, Lee HS, Kim JT, Kim SJ, Choi SH, Kang SG, Lee JH
    Ref: Applied Microbiology & Biotechnology, 93:623, 2012 : PubMed

            

&gt; Structure scheme for GTSAGmotif
&gt; Structures for GTSAGmotif (5)
&gt; List of Gene_Locus for GTSAGmotif (112)


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FamilyHormone-sensitive_lipase_like
CommentSequence similarities between hormone-sensitive lipase and prokaryotic enzymes was dicovered by Langin and Holm and Hemila et al.. The family Corresponds to the Pfam entry Abhydrolase_3. For bacterial enzymes this family correspond to family IV of the classification of Arpigny et al 1999
InterproIPR013094 (Alpha/beta hydrolase fold-3), IPR002168 (Lipolytic enzyme), IPR033140 (Lipase_GDXG_put_SER_AS), IPR002168 (Lipase_GDXG_HIS_AS)Pdoc PDOC00903
PFamPF07859 (Abhydrolase_3)PrintsProsite PS01173, PS01174
EC no EC numberTables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
    Title: Hormone-sensitive lipase: sixty years later
    Recazens E, Mouisel E, Langin D
    Ref: Prog Lipid Res, :101084, 2020 : PubMed

            

    Title: Bacterial Hormone-Sensitive Lipases (bHSLs): Emerging Enzymes for Biotechnological Applications
    Kim TD
    Ref: J Microbiol Biotechnol, 27:1907, 2017 : PubMed

            

    Title: Adipose Tissue Deficiency of Hormone-Sensitive Lipase Causes Fatty Liver in Mice
    Xia B, Cai GH, Yang H, Wang SP, Mitchell GA, Wu JW
    Ref: PLoS Genet, 13:e1007110, 2017 : PubMed

            

    Title: Molecular cloning and characterization of a thermostable carboxylesterase from an archaeon, Sulfolobus shibatae DSM5389: non-linear kinetic behavior of a hormone-sensitive lipase family enzyme
    Ejima K, Liu J, Oshima Y, Hirooka K, Shimanuki S, Yokota Y, Hemmi H, Nakayama T, Nishino T
    Ref: J Biosci Bioeng, 98:445, 2004 : PubMed

            

    Title: Structure-function relationships of hormone-sensitive lipase
    Osterlund T
    Ref: European Journal of Biochemistry, 268:1899, 2001 : PubMed

            

    Title: Molecular mechanisms regulating hormone-sensitive lipase and lipolysis
    Holm C, Osterlund T, Laurell H, Contreras JA
    Ref: Annu Rev Nutr, 20:365, 2000 : PubMed

            

    Title: Hormone-sensitive lipase is closely related to several bacterial proteins, and distantly related to acetylcholinesterase and lipoprotein lipase: identification of a superfamily of esterases and lipases
    Hemila H, Koivula TT, Palva I
    Ref: Biochimica & Biophysica Acta, 1210:249, 1994 : PubMed

            

    Title: Sequence similarities between hormone-sensitive lipase and five prokaryotic enzymes
    Langin D, Holm C
    Ref: Trends in Biochemical Sciences, 18:466, 1993 : PubMed

            

&gt; Structure scheme for Hormone-sensitive_lipase_like
&gt; Structures for Hormone-sensitive_lipase_like (114)
&gt; List of Gene_Locus for Hormone-sensitive_lipase_like (1623)


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FamilyKynurenine-formamidase
CommentKynurenine formamidase (EC:3.5.1.9) catalyses the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation. It is required for elimination of toxic metabolites
InterproIPR027519 (Kynurenine formamidase, vertebrates/fungi-type KFase_ver/fungi-typ)Pdoc
PFamPF07859 (Abhydrolase_3)PrintsProsite
ECAt KYOTO 3.5.1.9 at NYCEZYME 3.5.1.9Tables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
    Title: Biochemical identification and crystal structure of kynurenine formamidase from Drosophila melanogaster.
    Han Q, Robinson H, Li J
    Ref: Biochemical Journal, 446:253, 2012 : PubMed

            

    Title: Identification of formyl kynurenine formamidase and kynurenine aminotransferase from Saccharomyces cerevisiae using crystallographic, bioinformatic and biochemical evidence
    Wogulis M, Chew ER, Donohoue PD, Wilson DK
    Ref: Biochemistry, 47:1608, 2008 : PubMed

            

    Title: Crystal structure of an alpha/beta serine hydrolase (YDR428C) from Saccharomyces cerevisiae at 1.85 A resolution
    Arndt JW, Schwarzenbacher R, Page R, Abdubek P, Ambing E, Biorac T, Canaves JM, Chiu HJ, Dai X and Wilson IA <43 more author(s)>
    Ref: Proteins, 58:755, 2005 : PubMed

            

    Title: Biochemical and genetic characterization of kynurenine formamidase from Drosophila melanogaster
    Moore GP, Sullivan DT
    Ref: Biochemical Genetics, 16:619, 1978 : PubMed

            

&gt; Structure scheme for Kynurenine-formamidase
&gt; Structures for Kynurenine-formamidase (4)
&gt; List of Gene_Locus for Kynurenine-formamidase (364)


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FamilyPlant_carboxylesterase
CommentNo plant Carboxylesterase show the SEDCLYLN motif (prosite PS00941). These carboxylesterase are related to the Hormone sensitive lipase. Gibbereline Insensitive Dwarf1 GID1 has a primary structure similar to that of the hormone-sensitive lipase. Gibberellins (GAs) are tetracyclic, diterpenoid plant hormones, essential for many developmental processes in higher plants HSLs. The nuclear GA receptor evolved from an esterase. 2-hydroxyisoflavone dehydratase from leguminosae also belong to this family, in these particular enzymes the catalytic serine is replaced by threonine. In tulips tuliposide-converting enzyme (TCE) purified from tulip bulbs catalyzed the conversion of tuliposides to tulipalins.The lactone-forming carboxylesterases, specifically catalyzing intramolecular transesterification, but not hydrolysis
InterproIPR013094 (Alpha/beta hydrolase fold-3)Pdoc
PFamPF07859 (Abhydrolase_3)PrintsProsite
EC no EC numberTables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
    Title: Genome-wide expression analysis of carboxylesterase (CXE) gene family implies GBCXE49 functional responding to alkaline stress in cotton
    Rui C, Peng F, Fan Y, Zhang Y, Zhang Z, Xu N, Zhang H, Wang J, Li S and Ye W <7 more author(s)>
    Ref: BMC Plant Biol, 22:194, 2022 : PubMed

            

    Title: Evolution and diversification of the plant gibberellin receptor GID1
    Yoshida H, Tanimoto E, Hirai T, Miyanoiri Y, Mitani R, Kawamura M, Takeda M, Takehara S, Hirano K and Ueguchi-Tanaka M <3 more author(s)>
    Ref: Proc Natl Acad Sci U S A, 115:E7844, 2018 : PubMed

            

    Title: Molecular identification of tuliposide B-converting enzyme: a lactone-forming carboxylesterase from the pollen of tulip
    Nomura T, Murase T, Ogita S, Kato Y
    Ref: Plant J, 83:252, 2015 : PubMed

            

    Title: Molecular diversity of tuliposide A-converting enzyme in the tulip
    Nomura T, Tsuchigami A, Ogita S, Kato Y
    Ref: Biosci Biotechnol Biochem, 77:1042, 2013 : PubMed

            

    Title: Molecular determinants that convert hormone sensitive lipase into gibberellin receptor
    Hirano K, Aya K, Matsuoka M, Ueguchi-Tanaka M
    Ref: Protein Pept Lett, 19:180, 2012 : PubMed

            

    Title: A novel lactone-forming carboxylesterase: molecular identification of a tuliposide A-converting enzyme in tulip
    Nomura T, Ogita S, Kato Y
    Ref: Plant Physiol, 159:565, 2012 : PubMed

            

    Title: Gibberellin-induced DELLA recognition by the gibberellin receptor GID1
    Murase K, Hirano Y, Sun TP, Hakoshima T
    Ref: Nature, 456:459, 2008 : PubMed

            

    Title: Structural basis for gibberellin recognition by its receptor GID1
    Shimada A, Ueguchi-Tanaka M, Nakatsu T, Nakajima M, Naoe Y, Ohmiya H, Kato H, Matsuoka M
    Ref: Nature, 456:520, 2008 : PubMed

            

    Title: High-resolution crystal structure of plant carboxylesterase AeCXE1, from Actinidia eriantha, and its complex with a high-affinity inhibitor paraoxon
    Ileperuma NR, Marshall SD, Squire CJ, Baker HM, Oakeshott JG, Russell RJ, Plummer KM, Newcomb RD, Baker EN
    Ref: Biochemistry, 46:1851, 2007 : PubMed

            

    Title: Molecular and biochemical characterization of 2-hydroxyisoflavanone dehydratase. Involvement of carboxylesterase-like proteins in leguminous isoflavone biosynthesis
    Akashi T, Aoki T, Ayabe S
    Ref: Plant Physiol, 137:882, 2005 : PubMed

            

    Title: The carboxylesterase gene family from Arabidopsis thaliana
    Marshall SD, Putterill JJ, Plummer KM, Newcomb RD
    Ref: Journal of Molecular Evolution, 57:487, 2003 : PubMed

            

no Image
&gt; Structures for Plant_carboxylesterase (9)
&gt; List of Gene_Locus for Plant_carboxylesterase (501)


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FamilySteryl_acetyl_hydrolase
CommentSterol homeostasis in eukaryotic cells relies on the reciprocal interconversion of free sterols and steryl esters. In Saccharomyces cerevisiae (Baker's yeast) sterol acetylation requires the acetyltransferase Atf2, whereas deacetylation requires Say1, a membrane-anchored deacetylase with a putative active site in the ER lumen. Lack of Say1 results in the secretion of acetylated sterols into the culture medium, indicating that the substrate specificity of Say1 determines whether acetylated sterols are secreted from the cells or whether they are deacetylated and retained. In S. cerevisiae cells lacking Say1 or Atf2 are sensitive against the plant-derived allylbenzene eugenol and both Say1 and Atf2 affect pregnenolone toxicity, indicating that lipid acetylation acts as a detoxification pathway (old DUF2424)
InterproIPR019436 (Steryl_acetyl_hydrolase)Pdoc
PFamPF10340 (Say1_Mug180)PrintsProsite
EC no EC numberTables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
    Title: An acetylation/deacetylation cycle controls the export of sterols and steroids from S. cerevisiae
    Tiwari R, Koffel R, Schneiter R
    Ref: EMBO Journal, 26:5109, 2007 : PubMed

            

no Image
no Structure
&gt; List of Gene_Locus for Steryl_acetyl_hydrolase (64)


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FamilyTannase_Bact
CommentThis family of bacterial tannases close to hormone sensitive lipases, differs from the (Tannase) tannases and feruloyl esterase of fungi and bacteria grouped in the tannase family. The first structure described by Ren et al. Matoba et al. in this family presents a large cap domain inserted after the beta 7 strand of classical alpha/beta hydrolases. Tannases hydrolyze the galloyl ester bond in tannins to release gallic acid
InterproPdoc
PFamPrintsProsite
ECAt KYOTO 3.1.1.73 at NYCEZYME 3.1.1.73Tables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
    Title: Crystallographic and mutational analyses of tannase from Lactobacillus plantarum
    Matoba Y, Tanaka N, Noda M, Higashikawa F, Kumagai T, Sugiyama M
    Ref: Proteins, 81:2052, 2013 : PubMed

            

    Title: Crystal structure of tannase from lactobacillusplantarum
    Ren B, Wu M, Wang Q, Peng X, Wen H, McKinstry WJ, Chen Q
    Ref: Journal of Molecular Biology, 425:2737, 2013 : PubMed

            

no Image
&gt; Structures for Tannase_Bact (12)
&gt; List of Gene_Locus for Tannase_Bact (138)



Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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