Results 1 to 10 of about 2,184 (137)
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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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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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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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.
HIGUCHI, Takayoshi, SHIMADA, Mikio
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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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Food Science and Human WellnessGrass carp fillets were susceptible to unpleasant fishiness during cold storage. To clarify the mechanism of fishy odor formation and achieve targeted regulation, volatile compounds, and lipid oxidation were investigated in grass carp fillets during cold
Huifang Yang +4 more
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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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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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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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