Crystal structure of UDP-galactose 4-epimerase from the hyperthermophilic archaeon Pyrobaculum calidifontis

2011 ◽  
Vol 512 (2) ◽  
pp. 126-134 ◽  
Author(s):  
Haruhiko Sakuraba ◽  
Tomoyuki Kawai ◽  
Kazunari Yoneda ◽  
Toshihisa Ohshima
Keyword(s):  
Crystal Structure ◽  
Hyperthermophilic Archaeon ◽  
Pyrobaculum Calidifontis

The crystal structure of an esterase from the hyperthermophilic microorganism Pyrobaculum calidifontis VA1 explains its enantioselectivity

2011 ◽  
Vol 91 (4) ◽  
pp. 1061-1072 ◽  
Author(s):  
Gottfried J. Palm ◽  
Elena Fernández-Álvaro ◽  
Xenia Bogdanović ◽  
Sebastian Bartsch ◽  
Jaroslaw Sczodrok ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Pyrobaculum Calidifontis ◽  
Hyperthermophilic Microorganism

Pcal_1699, an extremely thermostable malate dehydrogenase from hyperthermophilic archaeon Pyrobaculum calidifontis

Extremophiles ◽  
2015 ◽  
Vol 20 (1) ◽  
pp. 57-67 ◽  
Author(s):  
Ghazaleh Gharib ◽  
Naeem Rashid ◽  
Qamar Bashir ◽  
Qura-tul Ann Afza Gardner ◽  
Muhammad Akhtar ◽  
...  
Keyword(s):  
Malate Dehydrogenase ◽  
Hyperthermophilic Archaeon ◽  
Pyrobaculum Calidifontis

scholarly journals Unique Presence of a Manganese Catalase in a Hyperthermophilic Archaeon, Pyrobaculum calidifontis VA1

2002 ◽  
Vol 184 (12) ◽  
pp. 3305-3312 ◽  
Author(s):  
Taku Amo ◽  
Haruyuki Atomi ◽  
Tadayuki Imanaka
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Catalase Activity ◽  
Specific Activity ◽  
Homology Search ◽  
Aerobic Conditions ◽  
Hyperthermophilic Archaeon ◽  
Manganese Catalase ◽  
Catalase Gene ◽  
Pyrobaculum Calidifontis

ABSTRACT We had previously isolated a facultatively anaerobic hyperthermophilic archaeon, Pyrobaculum calidifontis strain VA1. Here, we found that strain VA1, when grown under aerobic conditions, harbors high catalase activity. The catalase was purified 91-fold from crude extracts and displayed a specific activity of 23,500 U/mg at 70°C. The enzyme exhibited a Km value of 170 mM toward H2O2 and a k cat value of 2.9 × 104 s−1·subunit−1 at 25°C. Gel filtration chromatography indicated that the enzyme was a homotetramer with a subunit molecular mass of 33,450 Da. The purified catalase did not display the Soret band, which is an absorption band particular to heme enzymes. In contrast to typical heme catalases, the catalase was not strongly inhibited by sodium azide. Furthermore, with plasma emission spectroscopy, we found that the catalase did not contain iron but instead contained manganese. Our biochemical results indicated that the purified catalase was not a heme catalase but a manganese (nonheme) catalase, the first example in archaea. Intracellular catalase activity decreased when cells were grown anaerobically, while under aerobic conditions, an increase in activity was observed with the removal of thiosulfate from the medium, or addition of manganese. Based on the N-terminal amino acid sequence of the purified protein, we cloned and sequenced the catalase gene (katPc ). The deduced amino acid sequence showed similarity with that of the manganese catalase from a thermophilic bacterium, Thermus sp. YS 8-13. Interestingly, in the complete archaeal genome sequences, no open reading frame has been assigned as a manganese catalase gene. Moreover, a homology search with the sequence of katPc revealed that no orthologue genes were present on the archaeal genomes, including those from the “aerobic” (hyper)thermophilic archaea Aeropyrum pernix, Sulfolobus solfataricus, and Sulfolobus tokodaii. Therefore, Kat Pc can be considered a rare example of a manganese catalase from archaea.

scholarly journals Crystal structure of STS042, a stand-alone RAM module protein, from hyperthermophilic archaeon Sulfolobus tokodaii strain7

2008 ◽  
Vol 71 (3) ◽  
pp. 1557-1562 ◽  
Author(s):  
Ken-ichi Miyazono ◽  
Masanari Tsujimura ◽  
Yutaka Kawarabayasi ◽  
Masaru Tanokura
Keyword(s):  
Crystal Structure ◽  
Sulfolobus Tokodaii ◽  
Hyperthermophilic Archaeon

scholarly journals Crystal structure of archaeal phosphopantothenate synthetase

2014 ◽  
Vol 70 (a1) ◽  
pp. C455-C455
Author(s):  
Akiko Kita ◽  
Asako Kishimoto ◽  
Takuya Ishibashi ◽  
Hiroya Tomita ◽  
Yuusuke Yokooji ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Active Sites ◽  
Catalytic Mechanism ◽  
Rotation Axis ◽  
Structural Features ◽  
Common Pathway ◽  
Hyperthermophilic Archaeon ◽  
Pantothenate Synthetase ◽  
Almost All ◽  
Coenzyme A Biosynthesis

Bacteria/eukaryotes share a common pathway for coenzyme A biosynthesis which involves two enzymes, pantothenate synthetase and pantothenate kinase, to convert pantoate to 4'-phosphopantothenate. These two enzymes are absent in almost all archaea. Recently, it was reported that two novel enzymes, pantoate kinase (PoK) and phosphopantothenate synthetase (PPS), are responsible for this conversion in archaea[1]. In archaea, pantoate is phosphorylated by PoK to produce 4-phosphopantoate (PPo), and then condensation of PPo and β-alanine is catalyzed by PPS, generating 4'-phosphopantothenate. Here, we report the crystal structure of PPS from the hyperthermophilic archaeon, Thermococcus kodakarensis and its complexes with ATP, and ATP and 4-phosphopantoate (PPo). PPS forms an asymmetric homodimer, in which two monomers composing a dimer, deviated from the exact 2-fold symmetry, displaying 40-130distortion. Two active sites in PPS dimer are located near the rotation axis. Due to the asymmetricity of PPS dimer molecule, two active sites in PPS dimer are not equivalent. The structural features are consistent with the mutagenesis data and the results of biochemical experiments previously reported. Based on the structures of PPS, PPS/ATP complex, and PPS/ATP/PPo complex, we discuss the catalytic mechanism by which PPS produces phosphopantoyl adenylate (PPA), which is thought to be a reaction intermediate.

Refined crystal structure of a superoxide dismutase from the hyperthermophilic archaeon Sulfolobus acidocaldarius at 2.2 Å resolution 1 1Edited by R. Huber

1999 ◽  
Vol 285 (2) ◽  
pp. 689-702 ◽  
Author(s):  
Stefan Knapp ◽  
Simone Kardinahl ◽  
Niklas Hellgren ◽  
Gudrun Tibbelin ◽  
Günter Schäfer ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Superoxide Dismutase ◽  
Sulfolobus Acidocaldarius ◽  
Hyperthermophilic Archaeon

Catalytic properties and crystal structure of quinoprotein aldose sugar dehydrogenase from hyperthermophilic archaeon Pyrobaculum aerophilum

2010 ◽  
Vol 502 (2) ◽  
pp. 81-88 ◽  
Author(s):  
Haruhiko Sakuraba ◽  
Kaori Yokono ◽  
Kazunari Yoneda ◽  
Akira Watanabe ◽  
Yasuhiko Asada ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Catalytic Properties ◽  
Pyrobaculum Aerophilum ◽  
Hyperthermophilic Archaeon
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