Methanobacterium thermoautotrophicum (strain ΔH) contains a membrane-bound cyclic 2,3-diphosphoglycerate hydrolase

Alebeek, G.J.W.M. van; Kreuwels, M. J. J.; Keltjens, Jan T.; Vogels, Godfried D.

doi:10.1007/bf00307773

Cited by 4 publications

(3 citation statements)

References 22 publications

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“…Cobalt is used in a limited number of enzymes, unlike iron and zinc. However, there are several enzymes that are activated by cobalt ions: E. coli acetylornithinase [51], Methanobacterium thermoautotrophicum cyclic 2,3‐diphosphoglycerate hydrolase [52], and rat liver α‐ d ‐mannosidase [53]. However, it is not clear whether cobalt ions are involved in these enzymes.…”

Section: Resultsmentioning

confidence: 99%

Cobalt proteins

Kobayashi

Shimizu

1999

European Journal of Biochemistry

417

264

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In the form of vitamin B 12 , cobalt plays a number of crucial roles in many biological functions. However, recent studies have provided information on the biochemistry and bioinorganic chemistry of several proteins containing cobalt in a form other than that in the corrin ring of vitamin B 12 . To date, eight noncorrin-cobalt-containing enzymes (methionine aminopeptidase, prolidase, nitrile hydratase, glucose isomerase, methylmalonyl-CoA carboxytransferase, aldehyde decarbonylase, lysine-2,3-aminomutase, and bromoperoxidase) have been isolated and characterized. A cobalt transporter is involved in the metallocenter biosynthesis of the host cobalt-containing enzyme, nitrile hydratase. Understanding the differences between cobalt and nickel transporters might lead to drug development for gastritis and peptic ulceration.Keywords: cobalt; noncorrin; transporter; metal; inorganic chemistry; methionine aminopeptidase; prolidase; nitrile hydratase; glucose isomerase.Cobalt is a transition metal that occupies a position in the periodic table between iron and nickel. It has two naturally occurring oxidation states (Co 2+ and Co 3+ ), but can exhibit oxidation states from ±I to +IV. This metal is rare in comparison with all known essential trace elements except cadmium and tungsten: 0.0025% (w/w) in the Earth's crust and 4 £ 10 ±8 % (w/v) in sea water. Although cobalt is less frequently encountered in metalloenzymes than the other first-row transition metals (e.g. manganese, iron, copper and zinc), it is nevertheless an important cofactor in vitamin-B 12 -dependent enzymes. Vitamin B 12 [1] contains cobalt in a substituted corrin macrocycle (a porphyrin relative). The B 12 coenzyme possesses an axial Co(III)-alkyl (5 H -deoxyadenosine or methyl) group. Much effort has been concentrated on biochemical studies of this corrin cobalt. In contrast, only a few proteins containing noncorrin cobalt have been characterized.Radioactive cobalt ( 60 Co), which is produced by thermal neutron bombardment of the natural isotope 59 Co, has a half-life of 5.3 years and decays by b-and g-emission to nonradioactive nickel ( 60 Ni). It is used as a concentrated source of g radiation in cancer therapy and food sterilization, and as a radioactive tracer in biological and industrial applications [2]. Because cobalt has characteristic spectra correlated with structural properties (such as observed co-ordination numbers for Co 2+ and Co 3+ ), it has also served as a spectroscopic probe in metalloenzymes. Substituting cobalt for zinc has often been a useful tool to investigate the structural basis of catalytic properties in zinc enzymes and the co-ordination environment of active zinc sites in other proteins [3].Non-corrin cobalt is receiving increased interest not only in bioinorganic chemistry but also in biotechnology, and its availability and remarkable chemical versatility makes cobalt an invaluable catalyst in the chemical industry (e.g. hydroformylation as seen in the oxo process [4]). To date, eight noncorrin-cobalt-containing enzymes hav...

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Section: Resultsmentioning

confidence: 99%

Cobalt proteins

Kobayashi

Shimizu

1999

European Journal of Biochemistry

417

264

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“…The ability to generate ATP from ADP, inorganic phosphate Pi) and cDPG under these conditions could argue for a role in energy storage in that organism. However, in Methanobacter thermoautotrophicus , the K + -activated cDGPS appears irreversible (and membrane-bound), suggesting it may have a different role [105]. In soluble cell extracts, hydrolysis of cDPG in the presence of ADP and Pi could not generate ATP [106].…”

Section: Biosynthesis Of Osmolytes – Novel Pathways and Regulationmentioning

confidence: 99%

“…In soluble cell extracts, hydrolysis of cDPG in the presence of ADP and Pi could not generate ATP [106]. However, a membrane bound hydrolase that is inhibited by K + and Pi has also been identified [105]. The regulation of cDPG degradation in M. thermautotrophicus is consistent with it playing a role as a carbon and phosphate storage compound, although its high concentration in cells clearly indicates it contributes to osmotic balance.…”

Section: Biosynthesis Of Osmolytes – Novel Pathways and Regulationmentioning

confidence: 99%

Organic compatible solutes of halotolerant and halophilic microorganisms

2005

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Microorganisms that adapt to moderate and high salt environments use a variety of solutes, organic and inorganic, to counter external osmotic pressure. The organic solutes can be zwitterionic, noncharged, or anionic (along with an inorganic cation such as K(+)). The range of solutes, their diverse biosynthetic pathways, and physical properties of the solutes that effect molecular stability are reviewed.

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Activation and thermostabilization effects of cyclic 2,3-diphosphoglycerate on enzymes from the hyperthermophilic Methanopyrus kandleri

Shima¹,

Hérault

Berkessel

et al. 1998

Archives of Microbiology

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Enzymes involved in methane formation from carbon dioxide and dihydrogen in Methanopyrus kandleri require high concentrations (> 1 M) of lyotropic salts such as K2HPO4/KH2PO4 or (NH4)2SO4 for activity and for thermostability. The requirement correlates with high intracellular concentrations of cyclic 2,3-diphosphoglycerate (cDPG; approximately 1 M) in this hyperthermophilic organism. We report here on the effects of potassium cDPG on the activity and thermostability of the two methanogenic enzymes cyclohydrolase and formyltransferase and show that at cDPG concentrations prevailing in the cells the investigated enzymes are highly active and completely thermostable. At molar concentrations also the potassium salts of phosphate and of 2,3-bisphosphoglycerate, the biosynthetic precursor of cDPG, were found to confer activity and thermostability to the enzymes. Thermodynamic arguments are discussed as to why cDPG, rather than these salts, is present in high concentrations in the cells of Mp. kandleri.

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Methanobacterium thermoautotrophicum (strain ΔH) contains a membrane-bound cyclic 2,3-diphosphoglycerate hydrolase

Cited by 4 publications

References 22 publications

Cobalt proteins

Cobalt proteins

Organic compatible solutes of halotolerant and halophilic microorganisms

Activation and thermostabilization effects of cyclic 2,3-diphosphoglycerate on enzymes from the hyperthermophilic Methanopyrus kandleri

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