scholarly journals The crystal structure of a novel glucosamine-6-phosphate deaminase from the hyperthermophilic archaeon Pyrococcus furiosus

2007 ◽  
Vol 68 (1) ◽  
pp. 413-417 ◽  
Author(s):  
Kyung-Jin Kim ◽  
Myung Hee Kim ◽  
Ghyung-Hwa Kim ◽  
Beom Sik Kang
Keyword(s):  
Crystal Structure ◽  
Pyrococcus Furiosus ◽  
Hyperthermophilic Archaeon

scholarly journals The First Agmatine/Cadaverine Aminopropyl Transferase: Biochemical and Structural Characterization of an Enzyme Involved in Polyamine Biosynthesis in the Hyperthermophilic Archaeon Pyrococcus furiosus

2007 ◽  
Vol 189 (16) ◽  
pp. 6057-6067 ◽  
Author(s):  
Giovanna Cacciapuoti ◽  
Marina Porcelli ◽  
Maria Angela Moretti ◽  
Francesca Sorrentino ◽  
Luigi Concilio ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Active Site ◽  
Pyrococcus Furiosus ◽  
Limited Proteolysis ◽  
Stress Adaptation ◽  
Polyamine Biosynthesis ◽  
Hyperthermophilic Archaeon ◽  
Polyamine Content ◽  
Insight Into

ABSTRACT We report here the characterization of the first agmatine/cadaverine aminopropyl transferase (ACAPT), the enzyme responsible for polyamine biosynthesis from an archaeon. The gene PF0127 encoding ACAPT in the hyperthermophile Pyrococcus furiosus was cloned and expressed in Escherichia coli, and the recombinant protein was purified to homogeneity. P. furiosus ACAPT is a homodimer of 65 kDa. The broad substrate specificity of the enzyme toward the amine acceptors is unique, as agmatine, 1,3-diaminopropane, putrescine, cadaverine, and sym-nor-spermidine all serve as substrates. While maximal catalytic activity was observed with cadaverine, agmatine was the preferred substrate on the basis of the k cat/Km value. P. furiosus ACAPT is thermoactive and thermostable with an apparent melting temperature of 108°C that increases to 112°C in the presence of cadaverine. Limited proteolysis indicated that the only proteolytic cleavage site is localized in the C-terminal region and that the C-terminal peptide is not necessary for the integrity of the active site. The crystal structure of the enzyme determined to 1.8-Å resolution confirmed its dimeric nature and provided insight into the proteolytic analyses as well as into mechanisms of thermal stability. Analysis of the polyamine content of P. furiosus showed that spermidine, cadaverine, and sym-nor-spermidine are the major components, with small amounts of sym-nor-spermine and N-(3-aminopropyl)cadaverine (APC). This is the first report in Archaea of an unusual polyamine APC that is proposed to play a role in stress adaptation.

The Crystal Structure of a Virus-like Particle from the Hyperthermophilic Archaeon Pyrococcus furiosus Provides Insight into the Evolution of Viruses

2007 ◽  
Vol 368 (5) ◽  
pp. 1469-1483 ◽  
Author(s):  
Fusamichi Akita ◽  
Khoon Tee Chong ◽  
Hideaki Tanaka ◽  
Eiki Yamashita ◽  
Naoyuki Miyazaki ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Pyrococcus Furiosus ◽  
Hyperthermophilic Archaeon ◽  
Virus Like Particle ◽  
Evolution Of Viruses ◽  
Insight Into

scholarly journals Crystal Structure of a Novel Carboxypeptidase from the Hyperthermophilic Archaeon Pyrococcus furiosus

Structure ◽  
2002 ◽  
Vol 10 (2) ◽  
pp. 215-224 ◽  
Author(s):  
Joseph W. Arndt ◽  
Bing Hao ◽  
Vijay Ramakrishnan ◽  
Timothy Cheng ◽  
Sunney I. Chan ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Pyrococcus Furiosus ◽  
Hyperthermophilic Archaeon

scholarly journals A Novel DNA Polymerase Family Found inArchaea

1998 ◽  
Vol 180 (8) ◽  
pp. 2232-2236 ◽  
Author(s):  
Yoshizumi Ishino ◽  
Kayoko Komori ◽  
Isaac K. O. Cann ◽  
Yosuke Koga
Keyword(s):  
Escherichia Coli ◽  
Dna Polymerase ◽  
Pyrococcus Furiosus ◽  
Dna Polymerases ◽  
Open Reading Frames ◽  
Gene Products ◽  
Polymerase Gene ◽  
Hyperthermophilic Archaeon ◽  
Dna Polymerase Ii ◽  
Reading Frames

ABSTRACT One of the most puzzling results from the complete genome sequence of the methanogenic archaeon Methanococcus jannaschii was that the organism may have only one DNA polymerase gene. This is because no other DNA polymerase-like open reading frames (ORFs) were found besides one ORF having the typical α-like DNA polymerase (family B). Recently, we identified the genes of DNA polymerase II (the second DNA polymerase) from the hyperthermophilic archaeonPyrococcus furiosus, which has also at least one α-like DNA polymerase (T. Uemori, Y. Sato, I. Kato, H. Doi, and Y. Ishino, Genes Cells 2:499–512, 1997). The genes in M. jannaschiiencoding the proteins that are homologous to the DNA polymerase II ofP. furiosus have been located and cloned. The gene products of M. jannaschii expressed in Escherichia colihad both DNA polymerizing and 3′→5′ exonuclease activities. We propose here a novel DNA polymerase family which is entirely different from other hitherto-described DNA polymerases.

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
Sign in / Sign up

Export Citation Format

Share Document