The 1.5 Å resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic archaeon Pyrococcus furiosus , bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight into substrate binding and stability in carbamate kinases 1 1Edited by R. Huber

2000 ◽  
Vol 299 (2) ◽  
pp. 463-476 ◽  
Author(s):  
Santiago Ramón-Maiques ◽  
Alberto Marina ◽  
Matxalen Uriarte ◽  
Ignacio Fita ◽  
Vicente Rubio
Keyword(s):  
Crystal Structure ◽  
Pyrococcus Furiosus ◽  
Substrate Binding ◽  
Thermostable Enzyme ◽  
Carbamoyl Phosphate Synthetase ◽  
Carbamoyl Phosphate ◽  
Hyperthermophilic Archaeon ◽  
Carbamate Kinase ◽  
Insight Into

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 Product inhibition studies on bovine liver carbamoyl phosphate synthetase

1974 ◽  
Vol 141 (3) ◽  
pp. 817-824 ◽  
Author(s):  
Keith R. F. Elliott ◽  
Keith F. Tipton
Keyword(s):  
Inorganic Phosphate ◽  
Substrate Binding ◽  
Inorganic Ions ◽  
Bovine Liver ◽  
Product Inhibition ◽  
Carbamoyl Phosphate Synthetase ◽  
Carbamoyl Phosphate ◽  
Product Release ◽  
Proposed Model ◽  
Inhibition Studies

A study of the product-inhibition patterns of carbamoyl phosphate synthetase from bovine liver is reported. Inhibition by adenosine, AMP and inorganic ions is also reported. The results are in agreement with the previously proposed model in which the order of substrate binding is ATPMg, followed by HCO3−, ATPMg and NH4+. The order of product release on the basis of the reported results is carbamoyl phosphate, followed by ADPMg, ADPMg and inorganic phosphate.

Crystal Structure of α-Galactosidase from Lactobacillus acidophilus NCFM: Insight into Tetramer Formation and Substrate Binding

2011 ◽  
Vol 412 (3) ◽  
pp. 466-480 ◽  
Author(s):  
Folmer Fredslund ◽  
Maher Abou Hachem ◽  
René Jonsgaard Larsen ◽  
Pernille Gerd Sørensen ◽  
Pedro M. Coutinho ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Lactobacillus Acidophilus ◽  
Substrate Binding ◽  
Tetramer Formation ◽  
Lactobacillus Acidophilus Ncfm ◽  
Insight Into

[21] Carbamoyl phosphate synthesis: Carbamate kinase from Pyrococcus furiosus

2001 ◽  
pp. 236-247 ◽  
Author(s):  
Matxalen Uriarte ◽  
Alberto Marina ◽  
Santiago Ramón-Maiques ◽  
Vicente Rubio ◽  
Virginie Durbecq ◽  
...  
Keyword(s):  
Pyrococcus Furiosus ◽  
Carbamoyl Phosphate ◽  
Carbamate Kinase

scholarly journals The Carbamoyl-phosphate Synthetase ofPyrococcus furiosusIs Enzymologically and Structurally a Carbamate Kinase

1999 ◽  
Vol 274 (23) ◽  
pp. 16295-16303 ◽  
Author(s):  
Matxalen Uriarte ◽  
Alberto Marina ◽  
Santiago Ramón-Maiques ◽  
Ignacio Fita ◽  
Vicente Rubio
Keyword(s):  
Carbamoyl Phosphate Synthetase ◽  
Carbamoyl Phosphate ◽  
Carbamate Kinase
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