Genomic sequence of hyperthermophile, Pyrococcus furiosus: Implications for physiology and enzymology

Robb, Frank T.; Maeder, Dennis; Brown, James R.; DiRuggiero, Jocelyne; Stump, Mark; Yeh, Raymond; Weiss, Robert B.; Dunn, Dianne M.

doi:10.1016/s0076-6879(01)30372-5

Cited by 197 publications

(149 citation statements)

References 35 publications

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“…NA1, growing at high temperatures (70-90 C), and, by analyzing the genome sequence, we found that the open reading frame, composed of 1,497 bp, encodes a protein homologous to thermostable carboxypeptidase 1, which were purified and characterized from P. furiosus DSM 3638 (84% identity), 15,16) T. aquaticus YT-1 (35% identity), 17) and T. thermophilus HB27 (35% identity) 3) (Fig. 1).…”

Section: Resultsmentioning

confidence: 99%

Overexpression and Characterization of a Carboxypeptidase from the Hyperthermophilic ArchaeonThermococcussp. NA1

Lee¹,

Kim²,

Bae³

et al. 2006

Bioscience, Biotechnology, and Biochemistry

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Section: Resultsmentioning

confidence: 99%

Overexpression and Characterization of a Carboxypeptidase from the Hyperthermophilic ArchaeonThermococcussp. NA1

Lee¹,

Kim²,

Bae³

et al. 2006

Bioscience, Biotechnology, and Biochemistry

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“…We discuss this finding below. In the literature, a Nox enzyme from P. furiosus has been called Nox1 (Ward et al, 2001) and NoxA-3 (Maeder et al, 1999;Robb et al, 2001); we refer to this enzyme as NoxA-3. Group 3 of the FDR family includes NADH oxidases (Nox), NADH peroxidases (Npx) and CoADRs (Argyrou & Blanchard, 2004;Claiborne et al, 1999) (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…Methanogens are strict anaerobes (Boone et al, 1993). All anaerobic nonmethanogenic archaea examined thus far also carry Nox homologues (Klenk et al, 1997;Maeder et al, 1999;Robb et al, 2001). Since the Noxs of bacteria and eukaryotes catalyse the reduction of molecular oxygen (O 2 ) by either a two-electron transfer to produce hydrogen peroxide (H 2 O 2 ) or a four-electron transfer to produce H 2 O Toomey & Mayhew, 1998), it has been a puzzle why strictly anaerobic archaea carry Nox homologues.…”

Section: Introductionmentioning

confidence: 99%

“…The sources for the enzymes analysed are as follows (accession or ORF number; reference). MjNox, M. jannaschii Nox (MJ0649; Bult et al, 1996); PfNoxA-3, P. furiosus NoxA-3 (AAL81656; Maeder et al, 1999;Robb et al, 2001); AfNoxA-1, Archaeaglobus fulgidus NoxA-1 (AAB90976; Klenk et al, 1997); AfNoxA-2, A. fulgidus NoxA-2 (AAB90838; Klenk et al, 1997); EfNpx, Ent. faecalis NADH peroxidase (P37062; Ross & Claiborne, 1991); EfNox, Ent.…”

Section: Introductionmentioning

confidence: 99%

“…As a result it is unclear whether the nox homologue of M. jannaschii (mj0649) represents a disulfide reductase. Also, in contrast to non-methanogenic anaerobic archaea, which carry three to nine nox homologues (Klenk et al, 1997;Maeder et al, 1999;Robb et al, 2001), M. jannaschii carries only one such ORF (Pagala et al, 2002). Methanothermobacter thermautotrophicus, Methanococcus maripaludis, Methanosarcina acetivorans and Methanosarcina barkeri, which are also methanogens, carry one, one, two, and one Nox homologues, respectively (Galagan et al, 2002;Hendrickson et al, 2004; http://genome.ornl.gov/microbial/mbar/; Smith et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

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Characterization of an NADH oxidase of the flavin-dependent disulfide reductase family from Methanocaldococcus jannaschii

2009

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Methanocaldococcus jannaschii, a deeply rooted hyperthermophilic anaerobic methanarchaeon from a deep-sea hydrothermal vent, carries an NADH oxidase (Nox) homologue (MJ0649). According to the characteristics described here, MJ0649 represents an unusual member within group 3 of the flavin-dependent disulfide reductase (FDR) family. This FDR group comprises Nox, NADH peroxidases (Npx) and coenzyme A disulfide reductases (CoADRs); each carries a Cys residue that forms Cys-sulfenic acid during catalysis. A sequence analysis identified MJ0649 as a CoADR homologue. However, recombinant MJ0649 (rMJNox), expressed in Escherichia coli and purified to homogeneity an 86 kDa homodimer with 0.27 mol FAD (mol subunit) "1 , showed Nox but not CoADR activity. Incubation with FAD increased FAD content to 1 mol (mol subunit) "1 and improved NADH oxidase activity 3.4-fold. The FAD-incubated enzyme was characterized further. The optimum pH and temperature were ¢10 and ¢95 6C, respectively. At pH 7 and 83 6C, apparent K m values for NADH and O 2 were 3 mM and 1.9 mM, respectively, and the specific activity at 1.4 mM O 2 was 60 mmol min "1 mg "1 ; 62 % of NADH-derived reducing equivalents were recovered as H 2 O 2 and the rest probably generated H 2 O. rMjNox had poor NADPH oxidase, NADH peroxidase and superoxide formation activities. It reduced ferricyanide, plumbagin and 5,59-dithiobis(2-nitrobenzoic acid), but not disulfide coenzyme A and disulfide coenzyme M. Due to a high K m , O 2 is not a physiologically relevant substrate for MJ0649; its true substrate remains unknown.

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Pyruvate–Ferredoxin Oxidoreductase

Chabrière¹,

Cavazza²,

Contreras‐Martel³

2004

Handbook of Metalloproteins

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Introduction. Giardia intestinalis is a unicellular parasite of worldwide distribution. It causes an intestinal illness known as giardiasis, and it is probably the earliest diverging eukaryotic microorganism. Previously, changes have been reported in the expression of mRNAs at several stages of the life cycle; however specific enzymatic activity changes have not been explored. Objective. The expression of pyruvate ferredoxin oxidoreductase (PFOR) and alcohol dehydrogenase E (ADHE) enzymes was measured in cyst and trophozoite stages, and during the excystation process. Materials and methods. Recombinant proteins were generated for PFOR and ADHE to be used as antigens in the production of polyclonal antibodies for the detection of native proteins by Western Blot. The enzymatic activity of ADHE and glutamate dehydrogenase (GDH) was evaluated by spectrophotometric assays. Results. PFOR (139 kDa) and ADHE (97 kDa) proteins were detected in trophozoites, but not in cysts. During excystation, ADHE protein was detected after the first phase of induction, but the PFOR protein appeared only after the second phase. This indicated that both proteins were synthesized during excystation, although at different times. ADHE enzymatic activity was present only in trophozoites and not in cysts whereas GDH activity was detected in both stages. Conclusion. These results conclusively showed that PFOR and ADHE enzymes were translated during the excystation process and is strong evidence that active protein synthesis was occurring during excystation.

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Genomic sequence of hyperthermophile, Pyrococcus furiosus: Implications for physiology and enzymology

Cited by 197 publications

References 35 publications

Overexpression and Characterization of a Carboxypeptidase from the Hyperthermophilic ArchaeonThermococcussp. NA1

Overexpression and Characterization of a Carboxypeptidase from the Hyperthermophilic ArchaeonThermococcussp. NA1

Characterization of an NADH oxidase of the flavin-dependent disulfide reductase family from Methanocaldococcus jannaschii

Pyruvate–Ferredoxin Oxidoreductase

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