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6. Characterization of recombinant glutamine synthetase from the hyperthermophilic archaeon Pyrococcus sp. strain KOD1

Author

Rahman, Raja Noor Zaliha Abdul, Jongsareejit, Boonsri, Fujiwara, Shinsuke, and Imanaka, Tadayuki

Subjects
Ligases -- Research, Microbial enzymes -- Research, Bacteria, Thermophilic -- Research, Biological sciences
Abstract

The glnA gene encoding glutamine synthetase was cloned from the hyperthermophilic archaeon Pyrococcus sp. strain KOD1 and its nucleotide sequence was determined. The glnA gene was expressed in Escherichia coli ME8459 and the protein was purified to homogeneity and found to be functional in a dodecameric form, showing both transferase and synthetase activities. However, the enzyme had low biosynthetic activity, indicating that the reaction was biased towards glutamate production.

Published
1997

8. ScienceAsia

Author

Jongsareejit, Boonsri, primary, Bhumiratana, Amaret, additional, Morikawa, Masaaki, additional, and Kanaya, Shigenori, additional

Published
2007
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10. Application of N-terminally Truncated DNA Polymerase from Thermus thermophilus (ΔTth Polymerase) to DNA Sequencing and Polymerase Chain Reactions: Comparative Study of ΔTth and Wild-Type Tth Polymerases.

Author

Arakawa, Taku, Jongsareejit, Boonsri, Tatsumi, Yusaku, Tanaka, Keiko, Ikeda, Katsunori, Komatsubara, Hideyuki, Inoue, Hiroaki, Kawakami, Bunsei, Oka, Masanori, Emi, Shigenori, Yomo, Tetsuya, Shima, Yasufumi, Negoro, Seiji, and Urabe, Itaru

Abstract

N-Terminally truncated DNA polymerase from Thermus thermophilus (ΔTth polymerase) lacking 5′-3′ exonuclease activity was used for DNA sequencing and polymerase chain reaction (PCR). In contrast to the high background of the sequencing ladder observed with the wild-type Tth polymerase, ΔTth polymerase gave readable sequencing patterns which extend up to more than 500 bases from the primer site on cycle sequencing and automated sequencing. The ΔTth polymerase was used for the standard and mutagenic PCR, and net amplification of the DNA and the mutations accumulated during PCR were analyzed. Under mutagenic PCR, the mutation rates were 7.0 × 10−4 (Tth) and 8.3 × 10−4 (ΔTth) per nucleotide per cycle of amplification, which were 4–9 times higher than the rates under standard PCR. [ABSTRACT FROM PUBLISHER]

Published
1996
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11. Comparison of two glutamate producing enzymes from the hyperthermophilic archaeon Pyrococcussp. KOD1

Author

Jongsareejit, Boonsri, Fujiwara, Shinsuke, Takagi, Masahiro, and Imanaka, Tadayuki

Abstract

The glutamate dehydrogenase from Pyrococcussp. KOD1 (Pk‐GDH) was purified to homogeneity and its enzymatic characteristics for glutamate production were analyzed. Pk‐GDH exhibited glutamate producing activity from glutamine, which was found in some higher eukaryotic GDHs. However, the kcat/Kmvalues for ammonia and glutamine were 15×103min−1mM and 0.4×103min−1mM, respectively, indicating that the enzyme utilizes ammonia predominantly for glutamate production. Kinetic parameters of Pk‐GDH were compared with those of Pk‐GltA, which was previously identified as a glutamate synthase homologue. The turnover number for glutamine of Pk‐GltA (4.1×103min−1mM) was 10‐fold higher than that of Pk‐GDH (0.4×103min−1mM). Therefore, Pk‐GDH is less efficient than Pk‐GltA for glutamate production. Pk‐GDH utilized both NADPH and NADH as a cofactor, Pk‐GltA utilized only NADPH.

Published
1998
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12. Comparison of two glutamate producing enzymes from the hyperthermophilic archaeon Pyrococcus sp. KOD1

Author

Jongsareejit, Boonsri, Fujiwara, Shinsuke, Takagi, Masahiro, and Imanaka, Tadayuki

Abstract

The glutamate dehydrogenase from Pyrococcus sp. KOD1 (Pk-GDH) was purified to homogeneity and its enzymatic characteristics for glutamate production were analyzed. Pk-GDH exhibited glutamate producing activity from glutamine, which was found in some higher eukaryotic GDHs. However, the kcat/Km values for ammonia and glutamine were 15×103 min−1 mM and 0.4×103 min−1 mM, respectively, indicating that the enzyme utilizes ammonia predominantly for glutamate production. Kinetic parameters of Pk-GDH were compared with those of Pk-GltA, which was previously identified as a glutamate synthase homologue. The turnover number for glutamine of Pk-GltA (4.1×103 min−1 mM) was 10-fold higher than that of Pk-GDH (0.4×103 min−1 mM). Therefore, Pk-GDH is less efficient than Pk-GltA for glutamate production. Pk-GDH utilized both NADPH and NADH as a cofactor, Pk-GltA utilized only NADPH.

Published
1998
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