Results 131 to 140 of about 2,340 (183)

L-Fucose Metabolism in Mammals. I. Pork Liver L-Fuconate Hydro-lyase

Canadian Journal of Biochemistry, 1972
Pork liver has been shown to contain a soluble enzyme, L-fuconate hydro-lyase (L-fuconate dehydratase), capable of dehydrating L-fuconate to 2-keto-3-deoxy-L-fuconate. The enzyme has been partially purified. The Km for L-fuconate is 1.0 mM; D-arabonate is also an excellent substrate (Km 1.3 mM) but the enzyme is inactive with D-fuconate, L-arabonate ...
R, Yuen, H, Schachter
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Isolation and biochemical characterization of maleic‐acid hydratase, an iron‐requiring hydro‐lyase

European Journal of Biochemistry, 1985
A procedure for the isolation of maleic acid hydratase (D‐malete hydro‐lyase, EC 4.2.1.31) of about 95% purity from rabbit kidneys is described. The enzyme consists of a single polypeptide chain of 582 amino‐acid residues with an approximate molecular mass of 68 kDa.
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[Individuality of mannonate and altronate hydro-lyases in Escherichia coli K 12].

Biochimie, 1975
In Escherichia coli, mannonic and altronic hydrolyases act, respectively, on mannonate, the intermediate aldonate of the glucuronate branch, and on altronate the intermediate aldonate of the galacturonate branch of the hexuronate pathway, yielding 2-keto-3-deoxy-gluconate.
J M, Robert-Baudouy, J, Jimeno-Abendano, F R, Stoeber   +2 more
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The role of iron in the activation of mannoni and altronic acid hydratases, two Fe‐requiring hydro‐lyases

European Journal of Biochemistry, 1987
d‐Altronate hydratase and d‐mannonate hydratase belong to a class of Fe2+‐requiring enzymes, but the function of iron in these enzymes is largely unknown. Methods are described for the convenient preparation of both these hydratases from Escherichia coli and studies related to metal activation are presented.
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A study of the determination of 5-aminolevulinate hydro-lyase (δ-aminolevulinate dehydratase) activity in hemolysates of human erythrocytes

Clinical Biochemistry, 1971
Summary 1. The activity of 5-aminolevulinate hydro-lyase (δ-aminolevulinate dehydratase) has been determined in lysates of human erythrocytes through the rate of formation of porphobilinogen. The precision of the method was ±2 percent. 2. Dithiothreitol at 3 mmol/liter was an effective activator of the enzyme. 3.
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3-Indoleacetaldoxime hydro-lyase: A pyridoxal-5′-phosphate activated enzyme

Archives of Biochemistry and Biophysics, 1963
Kumar, SA, Mahadevan, S
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[Studies on the association of 5-dehydroquinate hydro-lyase and shikimate: NADP(+)-oxidoreductase in higher plants].

Planta, 2014
The properties of two enzymes involved in the shikimic acid pathway, dehydroquinate hydro-lyase and shikimate: NADP(+) oxidoreductase were studied in different species of higher plants (pteridophytes, gymnosperms, angiosperms) using chromatography on Sephadex G 100, DEAE cellulose, hydroxylapatite and isoelectric focusing.The two enzymes were not ...
A M, Boudet, R, Lécussan
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Global Atlas of Closed-Loop Pumped Hydro Energy Storage

Joule, 2021
Matthew Stocks, Ryan Stocks, Bin Lu
exaly  

[Formate dehydrogenase and formate hydro-lyase of Chloropseudomonas ethylica].

Mikrobiologiia, 1971
Z G, Tkacheva, E N, Kondrat'eva
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Zur Esterasewirkung der Carbonat-Hydro-Lyase aus Rindererythrozyten

Hoppe-Seyler´s Zeitschrift für physiologische Chemie, 1968
MANFRED LIEFLÄNDER, RONALD ZECH
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