Catalytic properties and crystal structure of thermostable NAD(P)H-dependent carbonyl reductase from the hyperthermophilic archaeon Aeropyrum pernix K1

2016 ◽  
Vol 91 ◽  
pp. 17-25 ◽  
Author(s):  
Yudai Fukuda ◽  
Haruhiko Sakuraba ◽  
Tomohiro Araki ◽  
Toshihisa Ohshima ◽  
Kazunari Yoneda
Keyword(s):  
Crystal Structure ◽  
Catalytic Properties ◽  
Carbonyl Reductase ◽  
Hyperthermophilic Archaeon ◽  
Aeropyrum Pernix

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

scholarly journals A novel NAD(P)H-dependent carbonyl reductase specifically expressed in the thyroidectomized chicken fatty liver: catalytic properties and crystal structure

FEBS Journal ◽  
2015 ◽  
Vol 282 (20) ◽  
pp. 3918-3928 ◽  
Author(s):  
Yudai Fukuda ◽  
Takeki Sone ◽  
Haruhiko Sakuraba ◽  
Tomohiro Araki ◽  
Toshihisa Ohshima ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Fatty Liver ◽  
Catalytic Properties ◽  
Carbonyl Reductase

Crystal structure of thioredoxin peroxidase from aerobic hyperthermophilic archaeon Aeropyrum pernix K1

2005 ◽  
Vol 62 (3) ◽  
pp. 822-826 ◽  
Author(s):  
Tsutomu Nakamura ◽  
Takahiko Yamamoto ◽  
Tsuyoshi Inoue ◽  
Hiroyoshi Matsumura ◽  
Atsuko Kobayashi ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Hyperthermophilic Archaeon ◽  
Aeropyrum Pernix ◽  
Thioredoxin Peroxidase

scholarly journals Insights into the Maturation of Pernisine, a Subtilisin-Like Protease from the Hyperthermophilic Archaeon Aeropyrum pernix

2020 ◽  
Vol 86 (17) ◽  
Author(s):  
Miha Bahun ◽  
Marko Šnajder ◽  
Dušan Turk ◽  
Nataša Poklar Ulrih
Keyword(s):  
High Temperature ◽  
High Temperatures ◽  
Catalytic Domain ◽  
Industrial Applications ◽  
Binding Motif ◽  
Content Type ◽  
Hyperthermophilic Archaeon ◽  
Aeropyrum Pernix ◽  
Autocatalytic Process ◽  
Exceptional Stability

ABSTRACT Pernisine is a subtilisin-like protease that was originally identified in the hyperthermophilic archaeon Aeropyrum pernix, which lives in extreme marine environments. Pernisine shows exceptional stability and activity due to the high-temperature conditions experienced by A. pernix. Pernisine is of interest for industrial purposes, as it is one of the few proteases that has demonstrated prion-degrading activity. Like other extracellular subtilisins, pernisine is synthesized in its inactive pro-form (pro-pernisine), which needs to undergo maturation to become proteolytically active. The maturation processes of mesophilic subtilisins have been investigated in detail; however, less is known about the maturation of their thermophilic homologs, such as pernisine. Here, we show that the structure of pro-pernisine is disordered in the absence of Ca2+ ions. In contrast to the mesophilic subtilisins, pro-pernisine requires Ca2+ ions to adopt the conformation suitable for its subsequent maturation. In addition to several Ca2+-binding sites that have been conserved from the thermostable Tk-subtilisin, pernisine has an additional insertion sequence with a Ca2+-binding motif. We demonstrate the importance of this insertion for efficient folding and stabilization of pernisine during its maturation. Moreover, analysis of the pernisine propeptide explains the high-temperature requirement for pro-pernisine maturation. Of note, the propeptide inhibits the pernisine catalytic domain more potently at high temperatures. After dissociation, the propeptide is destabilized at high temperatures only, which leads to its degradation and finally to pernisine activation. Our data provide new insights into and understanding of the thermostable subtilisin autoactivation mechanism. IMPORTANCE Enzymes from thermophilic organisms are of particular importance for use in industrial applications, due to their exceptional stability and activity. Pernisine, from the hyperthermophilic archaeon Aeropyrum pernix, is a proteolytic enzyme that can degrade infective prion proteins and thus has a potential use for disinfection of prion-contaminated surfaces. Like other subtilisin-like proteases, pernisine needs to mature through an autocatalytic process to become an active protease. In the present study, we address the maturation of pernisine and show that the process is regulated specifically at high temperatures by the propeptide. Furthermore, we demonstrate the importance of a unique Ca2+-binding insertion for stabilization of mature pernisine. Our results provide a novel understanding of thermostable subtilisin autoactivation, which might advance the development of these enzymes for commercial use.

The preparation and catalytic properties of copper(II) complexes derived from a pyrazole containing ligand. X-ray crystal structure of [Cu(pzmhp)(BF4)](BF4)

1997 ◽  
Vol 257 (1) ◽  
pp. 59-67 ◽  
Author(s):  
Mitchell R. Malachowski ◽  
Josephine Carden ◽  
Marilyn G. Davidson ◽  
Willem L. Driessen ◽  
Jan Reedijk
Keyword(s):  
Crystal Structure ◽  
Catalytic Properties ◽  
X Ray

scholarly journals Construction of an artificial biosynthetic pathway for hyperextended archaeal membrane lipids in the bacterium Escherichia coli

2020 ◽  
Vol 5 (1) ◽  
Author(s):  
Ryo Yoshida ◽  
Hisashi Hemmi
Keyword(s):  
Escherichia Coli ◽  
Biosynthetic Pathway ◽  
Membrane Lipids ◽  
Extreme Environments ◽  
Halophilic Archaea ◽  
Coli Strain ◽  
Glycerol Moiety ◽  
Hyperthermophilic Archaeon ◽  
E Coli ◽  
Aeropyrum Pernix

Abstract Archaea produce unique membrane lipids, which possess two fully saturated isoprenoid chains linked to the glycerol moiety via ether bonds. The isoprenoid chain length of archaeal membrane lipids is believed to be important for some archaea to thrive in extreme environments because the hyperthermophilic archaeon Aeropyrum pernix and some halophilic archaea synthesize extended C25,C25-archaeal diether-type membrane lipids, which have isoprenoid chains that are longer than those of typical C20,C20-diether lipids. Natural archaeal diether lipids possessing longer C30 or C35 isoprenoid chains, however, have yet to be isolated. In the present study, we attempted to synthesize such hyperextended archaeal membrane lipids. We investigated the substrate preference of the enzyme sn-2,3-(digeranylfarnesyl)glycerol-1-phosphate synthase from A. pernix, which catalyzes the transfer of the second C25 isoprenoid chain to the glycerol moiety in the biosynthetic pathway of C25,C25-archaeal membrane lipids. The enzyme was shown to accept sn-3-hexaprenylglycerol-1-phosphate, which has a C30 isoprenoid chain, as a prenyl acceptor substrate to synthesize sn-2-geranylfarnesyl-3-hexaprenylglycerol-1-phosphate, a supposed precursor for hyperextended C25,C30-archaeal membrane lipids. Furthermore, we constructed an artificial biosynthetic pathway by introducing 4 archaeal genes and 1 gene from Bacillus subtilis in the cells of Escherichia coli, which enabled the E. coli strain to produce hyperextended C25,C30-archaeal membrane lipids, which have never been reported so far.

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