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.
D. Flint, J. F. Tuminello, M. Emptage
exaly +5 more sources
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 ...
Roger Jeffcoat
core +6 more sources
Identification of two [4Fe-4S]-cluster-containing hydro-lyases from Pyrococcus furiosus.
Microbiology, 2009 The hyperthermophilic archaeonPyrococcus furiosusis a strict anaerobe. It is therefore not expected to use the oxidative tricarboxylic acid (TCA) cycle for energy transduction. Nonetheless, its genome encodes more putative TCA cycle enzymes than the closely relatedPyrococcus horikoshiiandPyrococcus abyssi, including an aconitase (PF0201).
B. V. van Vugt-Lussenburg +3 more
semanticscholar +4 more sources
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.
Ofelia L. Clara de Barreiro
openalex +5 more sources
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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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.
Roger Jeffcoat, H. Hassall, S. Dagley
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Isolation and biochemical characterization of maleic‐acid hydratase, an iron‐requiring hydro‐lyase [PDF]
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.
Jean-Luc Dreyer
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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
+4 more sources
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.
Roger Jeffcoat
openalex +3 more sources
Contribution of a Cyanide-insensitive Alternate Respiratory System to Increases in Formamide Hydro-lyase Activity and to Growth in Stemphylium loti in Vitro [PDF]
Plant Physiology, 1977 Stemphylium loti, a pathogen of a cyanogenic plant, possesses a cyanide-insensitive alternate respiratory pathway. In the absence of cytochrome inhibitors, the alternate system had only a minor role in respiration. When S. loti was grown in medium amended with antimycin to block the cytochrome chain, the alternate system accounted for the total oxygen ...
Jane F. Rissler, R. L. Millar
openalex +4 more sources