Results 1 to 10 of about 2,139 (119)
5-Aminolaevulinate hydro-lyase from yeast isolation and purification [PDF]
Biochimica et Biophysica Acta (BBA) - Enzymology, 1967 Une enzyme, l'aminolévulinate déshydratase (5-aminolévulinate hydro-lyase (addition de 5-aminolévulinate et cyclisation), EC 4.2.1.24) , qui catalyse la réaction suivante : a été isolée à partir de levure. Sa purification et certaines de ses propriétés ont été étudiées.
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Purification and properties of
Biochemical Journal, 1969 1. An enzyme extracted from Pseudomonas acidovorans was purified and shown to catalyse the simultaneous dehydration and decarboxylation of d-4-deoxy-5-oxoglucarate. It is proposed to name the enzyme d-4-deoxy-5-oxoglucarate hydro-lyase (decarboxylating), trivial name ‘deoxyoxoglucarate dehydratase’. 2.
R, Jeffcoat, H, Hassall, S, Dagley
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Journal of Hazardous Materials LettersPolylactic acid (PLA), the most popular bioplastic, has high sustainability potential as it is bio-sourced and also harbors biodegradability. A form of its biodegradability is via composting, and it was previously established that thermophilic ...
Shu Wei Hsueh +5 more
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Assay and Purification of (+)-Citramalate Hydro-lyase Components from Clostridium tetanomorphum
Journal of Biological Chemistry, 1966 The enzyme system ((+)-citramalate hydro-lyase, also called mesaconase) from Clostridium tetanomorphum, that catalyzes the reversible hydration of mesaconate to (+)-citramalate has been studied. A rapid, spectrophotometric assay for this activity has been developed, based upon the absorbance increase at 250 mµ when citramalate is converted to ...
A H, Blair, H A, Barker
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Applied SciencesAdvances in metagenomics have revolutionized our ability to elucidate links between the microbiome and human diseases. Colorectal cancer (CRC), a leading cause of cancer-related mortality worldwide, has been associated with dysbiosis of the gut ...
Burcu Bakir-Gungor +2 more
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The inactivation of Fe-S cluster containing hydro-lyases by superoxide.
Journal of Biological Chemistry, 1993 We report in this paper that highly purified Escherichia coli dihydroxy-acid dehydratase, fumarase A, fumarase B, and mammalian aconitase are inactivated by O2- with second order rate constants in the range of 10(6) to 10(7) M-1 s-1. Each of these enzymes belongs to the hydro-lyase class and contains catalytically active [4Fe-4S] clusters. Simultaneous
D H, Flint, J F, Tuminello, M H, Emptage
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Changes in Activity of 5-Dehydroquinate Hydro-lyase in Relation to Lignification of Bamboo [PDF]
Agricultural and Biological Chemistry, 1967 Characterization of 5-dehydroquinate hydro-lyase extracted from bomboo shoot was carried out. The enzyme was active over a broad range of pH with no marked peak between pH 6.0 and 8.0. Michaelis constant (Km) for dehydroquinic acid was found to be 1.3 × 10−5 m at pH 7.4.
Takayoshi Higuchi, Mikio Shimada
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Determination of Ultratrace Zinc by Enzymatic Activity of Carbonic Anhydrase. II. Use of Carbonate Hydro-lyase Activity [PDF]
Bulletin of the Chemical Society of Japan, 1981 Abstract A method for the determination of trace zinc has been investigated using hydro-lyase activity of carbonic anhydrase. It was proved theoretically and experimentally that the activation rate of the apo-carbonic anhydrase with zinc is proportional to the amount of zinc present in the solution.
Kensei Kobayashi +3 more
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Chemical Modification and Kinetic Studies on Glucarate Hydro‐Lyase from a Species of Pseudomonas A [PDF]
European Journal of Biochemistry, 1972 Glucarate hydro‐lyase, obtained from cells of Pseudomonas A grown on glucarate as the sole source of carbon, was purified 40‐fold in 70% yield. The effects of a variety of chemical modifiers and competitive inhibitors on the enzyme activity were studied.
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Studies on the subunit structure of 4-deoxy-5-oxoglucarate hydro-lyase (decarboxylating) from Pseudomonas acidovorans [PDF]
Biochemical Journal, 1975 1. Homogeneous preparations of D-4-deoxy-5-oxoglutarate hydro lyase (decarboxylating)(EC4.2.1.41) were analysed in the ultracentrifuge by the high-speed sedimentation-equilibrium method of Yphantis (1964). The molecular weight in 0.1 M-potassium phosphate buffer, pH 7.2, in 6M-guanidine hydrochloride and in 0.1 M-beta-mercaptoethanol in 6M-guanidine ...
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