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Purification and properties of extremely thermostable glutamate dehydrogenases from two hyperthermophilic archaebacteria, Pyrococcus woesei and Pyrococcus furiosus.
Two enzymes from the hyperthermophilic archaebacteria Pyrococcus woesei and P. furiosus were purified to homogeneity from crude extracts and had similar enzymological properties, however, some differences were detected in resistance to urea denaturation and effects of salts on their activity and stability. Expand
ADP-dependent Glucokinase/Phosphofructokinase, a Novel Bifunctional Enzyme from the Hyperthermophilic ArchaeonMethanococcus jannaschii *
The gene encoded in the hyperthermophilic archaeon Methanococcus jannaschii is proposed to be an ancestral gene of an ADP-dependent phosphofructokinase and glucokinase, and a gene duplication event might lead to the two enzymatic activities. Expand
Sequential Aldol Condensation Catalyzed by Hyperthermophilic 2-Deoxy-d-Ribose-5-Phosphate Aldolase
To the authors' surprise, the two hyperthermophilic DERAs showed much greater catalysis of sequential aldol condensation using three acetaldehydes as substrates than the E. coli DERA, although both enzymes showed much less 2-deoxy-d-ribose-5-phosphate synthetic activity. Expand
Biochemistry and biotechnology of amino acid dehydrogenases.
  • T. Ohshima, K. Soda
  • Biology, Medicine
  • Advances in biochemical engineering/biotechnology
  • 1990
The advances in biotechnological applications of amino acid dehydrogenases are based on fundamental studies concerning characteristics of the enzymes and reaction mechanism as described in this chapter. Expand
Crystal Structure of a Novel FAD-, FMN-, and ATP-containing l-Proline Dehydrogenase Complex from Pyrococcus horikoshii*
The structural characteristics of PDH1 suggest that each represents a divergent enzyme that arose from a common ancestral flavoenzyme and that they eventually formed a complex to gain a new function. Expand
Bilirubin Oxidase Activity of Bacillus subtilis CotA
This is the first characterization of bilirubin oxidase activity in a bacterial protein, and it is found that CotA from Bacillus subtilis shows strong bilirubsin oxid enzyme activity and markedly higher affinity for bilirUBin than conventional bilirube oxidase. Expand
Crystal Structure of the NAD Biosynthetic Enzyme Quinolinate Synthase*
The model of the catalytic state during the first condensation step of the quinolinate synthase reaction indicates that the elimination of inorganic phosphate from dihydroxyacetone phosphate may precede the condensation reaction. Expand
Dye-linked d-Proline Dehydrogenase from Hyperthermophilic Archaeon Pyrobaculum islandicum Is a Novel FAD-dependent Amino Acid Dehydrogenase*
The activity of dye-linkedd-proline dehydrogenase found in the crude extract of a hyperthermophilic archaeon, Pyrobaculum islandicum JCM 9189, shows that the membrane-bound d-prolinersase from Pb. Expand
Gene cloning and characterization of the very large NAD-dependent l-glutamate dehydrogenase from the psychrophile Janthinobacterium lividum, isolated from cold soil.
Surprisingly, NAD-GDH activity was markedly enhanced by the addition of various amino acids, such as l-aspartate and l-arginine, which strongly suggests that the N- and/or C-terminal domains play regulatory roles and are involved in the activation of the enzyme by these amino acids. Expand
Gene cloning and sequence determination of leucine dehydrogenase from Bacillus stearothermophilus and structural comparison with other NAD(P)+-dependent dehydrogenases.
Comparison of the amino acid sequence of leucine dehydrogenase with those of other pyridine nucleotide dependent oxidoreductases registered in a protein data bank revealed significant sequence similarity, particularly betweenLeucine and glutamate dehydrogenases, in the regions containing the coenzyme binding domain and certain specific residues with catalytic importance. Expand