NDLI: Cloning, expression, and structure analysis of carbamate kinase-like carbamoyl phosphate synthetase from Pyrococcus abyssi

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Cloning, expression, and structure analysis of carbamate kinase-like carbamoyl phosphate synthetase from Pyrococcus abyssi

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Cloning, expression, and structure analysis of carbamate kinase-like carbamoyl phosphate synthetase from Pyrococcus abyssi

Content Provider	Springer Nature Link
Author	Purcarea, Cristina Hervé, Guy Cunin, Raymond Evans, David R.
Copyright Year	2001
Abstract	Pyrococcus abyssi, a hyperthermophilic archaeon found in the vicinity of deep-sea hydrothermal vents, grows optimally at temperatures around 100°C. Carbamoyl phosphate synthetase (CPSase) from this organism was cloned and sequenced. The active 34-kDa recombinant protein was overexpressed in Escherichia coli when the host cells were cotransformed with a plasmid encoding tRNA synthetases for low-frequency Escherichia coli codons. Sequence homology suggests that the tertiary structure of P. abyssi CPSase, resembling its counterpart in Pyrococcus furiosus, is closely related to the catabolic carbamate kinases and is very different from the larger mesophilic CPSases. P. furiosus CPSase and carbamate kinase form carbamoyl phosphate by phosphorylating carbamate produced spontaneously in solution from ammonia and bicarbonate. In contrast, P. abyssi CPSase has intrinsic bicarbonate-dependent ATPase activity, suggesting that the enzyme can catalyze the phosphorylation of the isosteric substrates carbamate and bicarbonate.
Starting Page	229
Ending Page	239
Page Count	11
File Format	PDF
ISSN	14310651
Journal	Extremophiles
Volume Number	5
Issue Number	4
Language	English
Publisher	Springer-Verlag
Publisher Date	2001-07-04
Publisher Place	Tokyo
Access Restriction	One Nation One Subscription (ONOS)
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Medicine Microbiology

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Cloning, expression, and structure analysis of carbamate kinase-like carbamoyl phosphate synthetase from Pyrococcus abyssi

Structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic archaeon Pyrococcus furiosus bound to ADP

Metabolic Channeling of Carbamoyl Phosphate, a Thermolabile Intermediate EVIDENCE FOR PHYSICAL INTERACTION BETWEEN CARBAMATE KINASE-LIKE CARBAMOYL-PHOSPHATE SYNTHETASE AND ORNITHINE CARBAMOYLTRANSFERASE FROM THE HYPERTHERMOPHILE PYROCOCCUS FURIOSUS

The carbamate kinase-like carbamoyl phosphate synthetase of the hyperthermophilic archaeon Pyrococcus furiosus, a missing link in the evolution of carbamoyl phosphate biosynthesis.

Purification and Characterization of Carbamoyl-Phosphate Synthetase from the Deep-Sea Hyperthermophilic Archaebacterium Pyrococcus abyssi

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The carbamate kinase-like carbamoyl phosphate synthetase of the hyperthermophilic archaeon Pyrococcus furiosus, a missing link in the evolution of carbamoyl phosphate biosynthesis.

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Cloning, expression, and structure analysis of carbamate kinase-like carbamoyl phosphate synthetase from Pyrococcus abyssi

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