Tanokura M

References (14)

Title : Crystal structure and substrate recognition mechanism of the prolyl endoprotease PEP from Aspergillus niger - Miyazono_2022_Biochem.Biophys.Res.Commun_591_76
Author(s) : Miyazono KI , Kubota K , Takahashi K , Tanokura M
Ref : Biochemical & Biophysical Research Communications , 591 :76 , 2022
Abstract : Proteases are enzymes that are not only essential for life but also industrially important. Understanding the substrate recognition mechanisms of proteases is important to enhance the use of proteases. The fungus Aspergillus produces a wide variety of proteases, including PEP, which is a prolyl endoprotease from A. niger. Although PEP exhibits amino acid sequence similarity to the serine peptidase family S28 proteins (PRCP and DPP7) that recognize Pro-X bonds in the terminal regions of peptides, PEP recognizes Pro-X bonds not only in peptides but also in proteins. To reveal the structural basis of the prolyl endoprotease activity of PEP, we determined the structure of PEP by X-ray crystallography at a resolution of 1.75 A. The PEP structure shows that PEP has a wide-open catalytic pocket compared to its homologs. The characteristic catalytic pocket structure of PEP is predicted to be important for the recognition of protein substrates.
ESTHER : Miyazono_2022_Biochem.Biophys.Res.Commun_591_76
PubMedSearch : Miyazono_2022_Biochem.Biophys.Res.Commun_591_76
PubMedID: 34999257
Gene_locus related to this paper: aspnc-a2qr21

Title : Triazole Ureas Covalently Bind to Strigolactone Receptor and Antagonize Strigolactone Responses - Nakamura_2019_Mol.Plant_12_44
Author(s) : Nakamura H , Hirabayashi K , Miyakawa T , Kikuzato K , Hu W , Xu Y , Jiang K , Takahashi I , Niiyama R , Dohmae N , Tanokura M , Asami T
Ref : Mol Plant , 12 :44 , 2019
Abstract : Strigolactones, a class of plant hormones with multiple functions, mediate plant-plant and plant-microorganism communications in the rhizosphere. In this study, we developed potent strigolactone antagonists, which covalently bind to the strigolactone receptor D14, by preparing an array of triazole urea compounds. Using yeast two-hybrid and rice-tillering assays, we identified a triazole urea compound KK094 as a potent inhibitor of strigolactone receptors. Liquid chromatography-tandem mass spectrometry analysis and X-ray crystallography revealed that KK094 was hydrolyzed by D14, and that a reaction product of this degradation covalently binds to the Ser residue of the catalytic triad of D14. Furthermore, we identified two triazole urea compounds KK052 and KK073, whose effects on D14-D53/D14-SLR1 complex formation were opposite due to the absence (KK052) or presence (KK073) of a trifluoromethyl group on their phenyl ring. These results demonstrate that triazole urea compounds are potentially powerful tools for agricultural application and may be useful for the elucidation of the complicated mechanism underlying strigolactone perception.
ESTHER : Nakamura_2019_Mol.Plant_12_44
PubMedSearch : Nakamura_2019_Mol.Plant_12_44
PubMedID: 30391752
Gene_locus related to this paper: orysj-Q10QA5

Title : Structural analysis of HTL and D14 proteins reveals the basis for ligand selectivity in Striga - Xu_2018_Nat.Commun_9_3947
Author(s) : Xu Y , Miyakawa T , Nosaki S , Nakamura A , Lyu Y , Nakamura H , Ohto U , Ishida H , Shimizu T , Asami T , Tanokura M
Ref : Nat Commun , 9 :3947 , 2018
Abstract : HYPOSENSITIVE TO LIGHT (HTL) and DWARF14 (D14) mediate the perception of karrikin and strigolactone, which stimulates germination of the parasitic weed Striga. However, their role in parasitic seeds is poorly understood, and the basis for their differing responsiveness remains unclear. Here, we show that Striga hermonthica HTL proteins (ShHTLs) in 'conserved' and 'intermediate' clades are able to bind karrikin. The 'divergent' clade is able to hydrolyze strigolactone. Unexpectedly, we find that ShD14 is also capable of hydrolyzing strigolactone. Through comparative analysis of ShHTLs and ShD14 crystal structures, we provide insights into the basis for their selectivity. Moreover, we show that both ShD14 and divergent clade ShHTLs, but not conserved and intermediate clade ShHTLs, can interact with the putative downstream signaling component ShMAX2 in the presence of the synthetic strigolactone, rac-GR24. These findings provide insight into how strigolactone is perceived and how ligand specificity is determined.
ESTHER : Xu_2018_Nat.Commun_9_3947
PubMedSearch : Xu_2018_Nat.Commun_9_3947
PubMedID: 30258184
Gene_locus related to this paper: strhe-ShD14 , strhe-ShHTL4 , strhe-ShHTL1 , strhe-ShHTL7

Title : Methyl phenlactonoates are efficient strigolactone analogs with simple structure - Jamil_2018_J.Exp.Bot_69_2319
Author(s) : Jamil M , Kountche BA , Haider I , Guo X , Ntui VO , Jia KP , Ali S , Hameed US , Nakamura H , Lyu Y , Jiang K , Hirabayashi K , Tanokura M , Arold ST , Asami T , Al-Babili S
Ref : J Exp Bot , 69 :2319 , 2018
Abstract : Strigolactones (SLs) are a new class of phytohormones that also act as germination stimulants for root parasitic plants, such as Striga spp., and as branching factors for symbiotic arbuscular mycorrhizal fungi. Sources for natural SLs are very limited. Hence, efficient and simple SL analogs are needed for elucidating SL-related biological processes as well as for agricultural applications. Based on the structure of the non-canonical SL methyl carlactonoate, we developed a new, easy to synthesize series of analogs, termed methyl phenlactonoates (MPs), evaluated their efficacy in exerting different SL functions, and determined their affinity for SL receptors from rice and Striga hermonthica. Most of the MPs showed considerable activity in regulating plant architecture, triggering leaf senescence, and inducing parasitic seed germination. Moreover, some MPs outperformed GR24, a widely used SL analog with a complex structure, in exerting particular SL functions, such as modulating Arabidopsis roots architecture and inhibiting rice tillering. Thus, MPs will help in elucidating the functions of SLs and are promising candidates for agricultural applications. Moreover, MPs demonstrate that slight structural modifications clearly impact the efficiency in exerting particular SL functions, indicating that structural diversity of natural SLs may mirror a functional specificity.
ESTHER : Jamil_2018_J.Exp.Bot_69_2319
PubMedSearch : Jamil_2018_J.Exp.Bot_69_2319
PubMedID: 29300919

Title : Rationally Designed Strigolactone Analogs as Antagonists of the D14 Receptor - Takeuchi_2018_Plant.Cell.Physiol_59_1545
Author(s) : Takeuchi J , Jiang K , Hirabayashi K , Imamura Y , Wu Y , Xu Y , Miyakawa T , Nakamura H , Tanokura M , Asami T
Ref : Plant Cell Physiol , 59 :1545 , 2018
Abstract : Strigolactones (SLs) are plant hormones that inhibit shoot branching and act as signals in communications with symbiotic fungi and parasitic weeds in the rhizosphere. SL signaling is mediated by DWARF14 (D14), which is an alpha/beta-hydrolase that cleaves SLs into an ABC tricyclic lactone and a butenolide group (i.e. D-ring). This cleavage reaction (hydrolysis and dissociation) is important for inducing the interaction between D14 and its target proteins, including D3 and D53. In this study, a hydrolysis-resistant SL analog was predicted to inhibit the activation of the D14 receptor, thereby disrupting the SL signaling pathway. To test this prediction, carba-SL compounds, in which the ether oxygen of the D-ring or the phenol ether oxygen of the SL agonist (GR24 or 4-bromo debranone) was replaced with a methylene group, were synthesized as novel D14 antagonists. Subsequent biochemical and physiological studies indicated that carba-SLs blocked the interaction between D14 and D53 by inhibiting D14 hydrolytic activity. They also suppressed the SL-induced inhibition of rice tiller outgrowths. Additionally, carba-SLs antagonized the SL response in a Striga parasitic weed species. Structural analyses revealed that the D-ring of 7'-carba-4BD was hydrolyzed by D14 but did not dissociate from the 4BD skeleton. Thus, 7'-carba-4BD functioned as an antagonist rather than an agonist. Thus, the hydrolysis of the D-ring of SLs may be insufficient for activating the receptor. This study provides data relevant to designing SL receptor antagonists.
ESTHER : Takeuchi_2018_Plant.Cell.Physiol_59_1545
PubMedSearch : Takeuchi_2018_Plant.Cell.Physiol_59_1545
PubMedID: 29727000
Gene_locus related to this paper: arath-AtD14 , arath-KAI2.D14L

Title : Structural basis of unique ligand specificity of KAI2-like protein from parasitic weed Striga hermonthica - Xu_2016_Sci.Rep_6_31386
Author(s) : Xu Y , Miyakawa T , Nakamura H , Nakamura A , Imamura Y , Asami T , Tanokura M
Ref : Sci Rep , 6 :31386 , 2016
Abstract : The perception of two plant germination inducers, karrikins and strigolactones, are mediated by the proteins KAI2 and D14. Recently, KAI2-type proteins from parasitic weeds, which are possibly related to seed germination induced by strigolactone, have been classified into three clades characterized by different responses to karrikin/strigolactone. Here we characterized a karrikin-binding protein in Striga (ShKAI2iB) that belongs to intermediate-evolving KAI2 and provided the structural bases for its karrikin-binding specificity. Binding assays showed that ShKAI2iB bound karrikins but not strigolactone, differing from other KAI2 and D14. The crystal structures of ShKAI2iB and ShKAI2iB-karrikin complex revealed obvious structural differences in a helix located at the entry of its ligand-binding cavity. This results in a smaller closed pocket, which is also the major cause of ShKAI2iB's specificity of binding karrikin. Our structural study also revealed that a few non-conserved amino acids led to the distinct ligand-binding profile of ShKAI2iB, suggesting that the evolution of KAI2 resulted in its diverse functions.
ESTHER : Xu_2016_Sci.Rep_6_31386
PubMedSearch : Xu_2016_Sci.Rep_6_31386
PubMedID: 27507097
Gene_locus related to this paper: strhe-ShHTL3

Title : Structural basis for the Ca(2+)-enhanced thermostability and activity of PET-degrading cutinase-like enzyme from Saccharomonospora viridis AHK190 - Miyakawa_2015_Appl.Microbiol.Biotechnol_99_4297
Author(s) : Miyakawa T , Mizushima H , Ohtsuka J , Oda M , Kawai F , Tanokura M
Ref : Applied Microbiology & Biotechnology , 99 :4297 , 2015
Abstract : A cutinase-like enzyme from Saccharomonospora viridis AHK190, Cut190, hydrolyzes the inner block of polyethylene terephthalate (PET); this enzyme is a member of the lipase family, which contains an alpha/beta hydrolase fold and a Ser-His-Asp catalytic triad. The thermostability and activity of Cut190 are enhanced by high concentrations of calcium ions, which is essential for the efficient enzymatic hydrolysis of amorphous PET. Although Ca(2+)-induced thermostabilization and activation of enzymes have been well explored in alpha-amylases, the mechanism for PET-degrading cutinase-like enzymes remains poorly understood. We focused on the mechanisms by which Ca(2+) enhances these properties, and we determined the crystal structures of a Cut190 S226P mutant (Cut190(S226P)) in the Ca(2+)-bound and free states at 1.75 and 1.45 A resolution, respectively. Based on the crystallographic data, a Ca(2+) ion was coordinated by four residues within loop regions (the Ca(2+) site) and two water molecules in a tetragonal bipyramidal array. Furthermore, the binding of Ca(2+) to Cut190(S226P) induced large conformational changes in three loops, which were accompanied by the formation of additional interactions. The binding of Ca(2+) not only stabilized a region that is flexible in the Ca(2+)-free state but also modified the substrate-binding groove by stabilizing an open conformation that allows the substrate to bind easily. Thus, our study explains the structural basis of Ca(2+)-enhanced thermostability and activity in PET-degrading cutinase-like enzyme for the first time and found that the inactive state of Cut190(S226P) is activated by a conformational change in the active-site sealing residue, F106.
ESTHER : Miyakawa_2015_Appl.Microbiol.Biotechnol_99_4297
PubMedSearch : Miyakawa_2015_Appl.Microbiol.Biotechnol_99_4297
PubMedID: 25492421
Gene_locus related to this paper: sacvd-c7mve8

Title : A novel Ca-activated, thermostabilized polyesterase capable of hydrolyzing polyethylene terephthalate from Saccharomonospora viridis AHK190 - Kawai_2014_Appl.Microbiol.Biotechnol_98_10053
Author(s) : Kawai F , Oda M , Tamashiro T , Waku T , Tanaka N , Yamamoto M , Mizushima H , Miyakawa T , Tanokura M
Ref : Applied Microbiology & Biotechnology , 98 :10053 , 2014
Abstract : Only two polyethylene glycol terephthalate (PET)-degrading enzymes have been reported, and their mechanism for the biochemical degradation of PET remains unclear. To identify a novel PET-degrading enzyme, a putative cutinase gene (cut190) was cloned from the thermophile Saccharomonospora viridis AHK190 and expressed in Escherichia coli Rosetta-gami B (DE3). Mutational analysis indicated that substitution of Ser226 with Pro and Arg228 with Ser yielded the highest activity and thermostability. The Ca2+ ion enhanced the enzyme activity and thermostability of the wild-type and mutant Cut190. Circular dichroism suggested that the Ca2+ changes the tertiary structure of the Cut190 (S226P/R228S), which has optimal activity at 65-75 degrees C and pH 6.5-8.0 in the presence of 20 % glycerol. The enzyme was stable over a pH range of 5-9 and at temperatures up to 65 degrees C for 24 h with 40 % activity remaining after incubation for 1 h at 70 degrees C. The Cut190 (S226P/R228S) efficiently hydrolyzed various aliphatic and aliphatic-co-aromatic polyester films. Furthermore, the enzyme degraded the PET film above 60 degrees C. Therefore, Cut190 is the novel-reported PET-degrading enzyme with the potential for industrial applications in polyester degradation, monomer recycling, and PET surface modification. Thus, the Cut190 will be a useful tool to elucidate the molecular mechanisms of the PET degradation, Ca2+ activation, and stabilization.
ESTHER : Kawai_2014_Appl.Microbiol.Biotechnol_98_10053
PubMedSearch : Kawai_2014_Appl.Microbiol.Biotechnol_98_10053
PubMedID: 24929560
Gene_locus related to this paper: sacvd-c7mve8

Title : Crystal structure of the novel haloalkane dehalogenase DatA from Agrobacterium tumefaciens C58 reveals a special halide-stabilizing pair and enantioselectivity mechanism - Guan_2014_Appl.Microbiol.Biotechnol_98_8573
Author(s) : Guan L , Yabuki H , Okai M , Ohtsuka J , Tanokura M
Ref : Applied Microbiology & Biotechnology , 98 :8573 , 2014
Abstract : A novel haloalkane dehalogenase DatA from Agrobacterium tumefaciens C58 belongs to the HLD-II subfamily and hydrolyzes brominated and iodinated compounds, leading to the generation of the corresponding alcohol, a halide ion, and a proton. Because DatA possesses a unique Asn-Tyr pair instead of the Asn-Trp pair conserved among the subfamily members, which was proposed to keep the released halide ion stable, the structural basis for its reaction mechanism should be elucidated. Here, we determined the crystal structures of DatA and its Y109W mutant at 1.70 and 1.95 A, respectively, and confirmed the location of the active site by using its novel competitive inhibitor. The structural information from these two crystal structures and the docking simulation suggested that (i) the replacement of the Asn-Tyr pair with the Asn-Trp pair increases the binding affinity for some halogenated compounds, such as 1,3-dibromopropane, mainly due to the electrostatic interaction between Trp109 and halogenated compounds and the change of substrate-binding mode caused by the interaction and (ii) the primary halide-stabilizing residue is only Asn43 in the wild-type DatA, while Tyr109 is a secondary halide-stabilizing residue. Furthermore, docking simulation using the crystal structures of DatA indicated that its enantioselectivity is determined by the large and small spaces around the halogen-binding site.
ESTHER : Guan_2014_Appl.Microbiol.Biotechnol_98_8573
PubMedSearch : Guan_2014_Appl.Microbiol.Biotechnol_98_8573
PubMedID: 24770384
Gene_locus related to this paper: agrtu-DHAA

Title : Molecular mechanism of strigolactone perception by DWARF14 - Nakamura_2013_Nat.Commun_4_2613
Author(s) : Nakamura H , Xue YL , Miyakawa T , Hou F , Qin HM , Fukui K , Shi X , Ito E , Ito S , Park SH , Miyauchi Y , Asano A , Totsuka N , Ueda T , Tanokura M , Asami T
Ref : Nat Commun , 4 :2613 , 2013
Abstract : Strigolactones (SLs) are phytohormones that inhibit shoot branching and function in the rhizospheric communication with symbiotic fungi and parasitic weeds. An alpha/beta-hydrolase protein, DWARF14 (D14), has been recognized to be an essential component of plant SL signalling, although its precise function remains unknown. Here we present the SL-dependent interaction of D14 with a gibberellin signalling repressor SLR1 and a possible mechanism of phytohormone perception in D14-mediated SL signalling. D14 functions as a cleavage enzyme of SLs, and the cleavage reaction induces the interaction with SLR1. The crystal structure of D14 shows that 5-hydroxy-3-methylbutenolide (D-OH), which is a reaction product of SLs, is trapped in the catalytic cavity of D14 to form an altered surface. The D14 residues recognizing D-OH are critical for the SL-dependent D14-SLR1 interaction. These results provide new insight into crosstalk between gibberellin and SL signalling pathways.
ESTHER : Nakamura_2013_Nat.Commun_4_2613
PubMedSearch : Nakamura_2013_Nat.Commun_4_2613
PubMedID: 24131983
Gene_locus related to this paper: orysj-Q10QA5

Title : Crystal Structure and Site-Directed Mutagenesis Analyses of Haloalkane Dehalogenase LinB from Sphingobium sp. Strain MI1205 - Okai_2013_J.Bacteriol_195_2642
Author(s) : Okai M , Ohtsuka J , Imai LF , Mase T , Moriuchi R , Tsuda M , Nagata K , Nagata Y , Tanokura M
Ref : Journal of Bacteriology , 195 :2642 , 2013
Abstract : The enzymes LinBUT and LinBMI (LinB from Sphingobium japonicum UT26 and Sphingobium sp. MI1205, respectively) catalyze the hydrolytic dechlorination of beta-hexachlorocyclohexane (beta-HCH) and yield different products, 2,3,4,5,6-pentachlorocyclohexanol (PCHL) and 2,3,5,6-tetrachlorocyclohexane-1,4-diol (TCDL), respectively, despite their 98% identity in amino acid sequence. To reveal the structural basis of their different enzymatic properties, we performed site-directed mutagenesis and X-ray crystallographic studies of LinBMI and its seven point mutants. The mutation analysis revealed that the seven amino acid residues uniquely found in LinBMI were categorized into three groups based on the efficiency of the first-step (from beta-HCH to PCHL) and second-step (from PCHL to TCDL) conversions. Crystal structure analyses of wild-type LinBMI and its seven point mutants indicated how each mutated residue contributed to the first- and second-step conversions by LinBMI. The dynamics simulation analyses of wild-type LinBMI and LinBUT revealed that the entrance of the substrate access tunnel of LinBUT was more flexible than that of LinBMI, which could lead to the different efficiencies of dehalogenation activity between these dehalogenases.
ESTHER : Okai_2013_J.Bacteriol_195_2642
PubMedSearch : Okai_2013_J.Bacteriol_195_2642
PubMedID: 23564170
Gene_locus related to this paper: sphpi-q6vqx3

Title : Crystallization and preliminary X-ray analysis of the haloalkane dehalogenase DatA from Agrobacterium tumefaciens C58 - Mase_2012_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_68_652
Author(s) : Mase T , Yabuki H , Okai M , Ohtsuka J , Imai FL , Nagata Y , Tanokura M
Ref : Acta Crystallographica Sect F Struct Biol Cryst Commun , 68 :652 , 2012
Abstract : Haloalkane dehalogenases are enzymes that catalyze the hydrolytic reaction of a wide variety of haloalkyl substrates to form the corresponding alcohol and hydrogen halide products. DatA from Agrobacterium tumefaciens C58 is a haloalkane dehalogenase that has a unique pair of halide-binding residues, asparagine (Asn43) and tyrosine (Tyr109), instead of the asparagine and tryptophan that are conserved in other members of the subfamily. DatA was expressed in Escherichia coli, purified and crystallized using the sitting-drop vapour-diffusion method with a reservoir solution consisting of 0.1 M CHES pH 8.6, 1.0 M potassium sodium tartrate, 0.2 M lithium sulfate, 0.01 M barium chloride. X-ray diffraction data were collected to 1.70 A resolution. The space group of the crystal was determined as the primitive tetragonal space group P422, with unit-cell parameters a = b = 123.7, c = 88.1 A. The crystal contained two molecules in the asymmetric unit.
ESTHER : Mase_2012_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_68_652
PubMedSearch : Mase_2012_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_68_652
PubMedID: 22684062

Title : Autism spectrum disorder is related to endoplasmic reticulum stress induced by mutations in the synaptic cell adhesion molecule, CADM1 - Fujita_2010_Cell.Death.Dis_1_e47
Author(s) : Fujita E , Dai H , Tanabe Y , Zhiling Y , Yamagata T , Miyakawa T , Tanokura M , Momoi MY , Momoi T
Ref : Cell Death Dis , 1 :e47 , 2010
Abstract : Autism spectrum disorder (ASD) is a neurodevelopmental disorder with an unknown molecular pathogenesis. A recent molecular focus has been the mutated neuroligin 3, neuroligin 3(R451C), in gain-of-function studies and for its role in induced impairment of synaptic function, but endoplasmic reticulum (ER) stress induced by mutated molecules also deserves investigation. We previously found two missense mutations, H246N and Y251S, in the gene-encoding synaptic cell adhesion molecule-1 (CADM1) in ASD patients, including cleavage of the mutated CADM1 and its intracellular accumulation. In this study, we found that the mutated CADM1 showed slightly reduced homophilic interactions in vitro but that most of its interactions persist. The mutated CADM1 also showed morphological abnormalities, including shorter dendrites, and impaired synaptogenesis in neurons. Wild-type CADM1 was partly localized to the ER of C2C5 cells, whereas mutated CADM1 mainly accumulated in the ER despite different sensitivities toward 4-phenyl butyric acid with chemical chaperone activity and rapamycin with promotion activity for degradation of the aggregated protein. Modeling analysis suggested a direct relationship between the mutations and the conformation alteration. Both mutated CADM1 and neuroligin 3(R451C) induced upregulation of C/EBP-homologous protein (CHOP), an ER stress marker, suggesting that in addition to the trafficking impairment, this CHOP upregulation may also be involved in ASD pathogenesis.
ESTHER : Fujita_2010_Cell.Death.Dis_1_e47
PubMedSearch : Fujita_2010_Cell.Death.Dis_1_e47
PubMedID: 21364653

Title : Crystal structure of the proline iminopeptidase-related protein TTHA1809 from Thermus thermophilus HB8 - Okada_2008_J.Food.Sci_73_C146
Author(s) : Okai M , Miyauchi Y , Ebihara A , Lee WC , Nagata K , Tanokura M
Ref : Proteins , 70 :1646 , 2008
Abstract : Thermus thermophilus HB8, an extremely thermophilic bacterium. The open reading frame of TTHA1809 from Thermus thermophilus HB8 was annotated as a proline iminopeptidase-related protein. Proline iminopeptidase (PIP) is a serine peptidase that catalyzes the removal of N-terminal proline from peptides with high specificity. In this study, we report the crystal structure of the proline iminopeptidase-related protein TTHA1809 from Thermus thermophilus HB8, and compare the active site of the tricorn-interacting aminopeptidase F1, which is the best homolog found using the Dali program, with the corresponding region of TTHA1809. Comparison with the tricorn-interacting aminopeptidase F1: The tricorn-interacting aminopeptidase F120 from Thermoplasma acidophilum has a Ser-His-Asp catalytic triad in the active site. The superimposition between TTHA1809 and F1 revealed that the residue corresponding to the catalytic Ser105 in F1 is replaced by a Gly at TTHA1809. Asp229 and His255 of TTHA1809 were located at the same position as Asp244 and His271 of the catalytic triad of F1. His255 of TTHA1809 was located in a loop between the beta8-strand and the alpha10-helix. The ND-1 atom of His255 was hydrogen-bonded to Asp229 in a loop located between the beta7-strand and the alpha9-helix, whereas the NE-2 atom of His255 formed a hydrogen bond with a water molecule because of the lack of catalytic Ser residue. Thus, TTHA1809 and F1 would have different functions. A BLAST search using TTHA1809 revealed the possibility of the existence of enzymes lacking a catalytic Ser residue in several microorganisms (Thermus thermophilus HB27, Deinococcus geothermalis DSM 11300, Legionella pneumophila subsp. pneumophila str. Philadelphia 1, Dechloromonas aromatica RCB, and Hahella chejuensis KCTC 2396), but their functions have not yet been revealed.
ESTHER : Okada_2008_J.Food.Sci_73_C146
PubMedSearch : Okada_2008_J.Food.Sci_73_C146
PubMedID: 18175319
Gene_locus related to this paper: thet2-q72hm9