Results 11 to 20 of about 79,428 (144)
Scientific Reports, 2015 The bacteriophage encoded hyaluronate lyases (HylP and HylP2) degrade hyaluronan and other glycosaminoglycans. HylP2 forms a functional fibril under acidic conditions in which its N-terminus is proposed to form the fibrillar core, leading to nucleation ...
Harish Shukla +4 more
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Effects of Certain Hydroxamic Acids on L-Glutamate 1-Carboxy-lyase
Experimental Biology and Medicine, 1969 SummaryOver 50 hydroxamic acids (HA) were surveyed for inhibitory action against bacterial and vegetable glutamic acid carboxy-lyase (GCL). Appreciable activity against the bacterial enzyme was shown by 7 compounds. These 7, in addition to 2 others, also inhibited the vegetable enzyme.
J A, Howle, G R, Gale
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New Family of Ulvan Lyases Identified in Three Isolates from the Alteromonadales Order*
Journal of Biological Chemistry, 2016 Ulvan is the main polysaccharide component of the Ulvales (green seaweed) cell wall. It is composed of disaccharide building blocks comprising 3-sulfated rhamnose linked to d-glucuronic acid (GlcUA), l-iduronic acid (IdoUA), or d-xylose (Xyl).
Moran Kopel +5 more
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Identification of the active site residues in ATP‐citrate lyase's carboxy‐terminal portion
Protein Science, 2019 ATP‐citrate lyase (ACLY) catalyzes production of acetyl‐CoA and oxaloacetate from CoA and citrate using ATP. In humans, this cytoplasmic enzyme connects energy metabolism from carbohydrates to the production of lipids.
V. H. Nguyen +4 more
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Separation and allosteric properties of two forms of UDP-glucuronate carboxy-lyase.
Journal of Biological Chemistry, 1977 DEAE-cellulose chromatography of partially purified preparations of UDP-glucuronate carboxy-lyase from wheat germ results in the separation of two forms of the enzyme. Both are fully active in the absence of added DPN, have indistinguishable molecular weights (210,000), but differ in charge and kinetic properties.
K V, John, J S, Schutzbach, H, Ankel
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Porphyria‐induced hepatic porphyrinogen carboxy‐lyase inhibitor and its interaction with the active site(s) of the enzyme [PDF]
IUBMB Life, 1999 AbstractPorphyrinogen carboxy‐lyase is an enzyme that sequentially decarboxylates uroporphyrinogen III (8‐COOH) to yield coproporphyrinogen III (4‐COOH). In mammals this enzyme activity is impaired by hexachlorobenzene treatment, through generation of an enzyme inhibitor.
S B, de Catabbi +4 more
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Stereochemistry of Reactions Catalysed by Mammalian‐Brain
European Journal of Biochemistry, 1979 Deamination of 4‐aminobutyrate by mammalian or bacterial 4‐aminobutyrate aminotransferases involves the abstraction of the pro‐S hydrogen on C‐4 of 4‐aminobutyrate. Decarboxylation of L‐glutamate by rat brain glutamate decarboxylase occurs with retention of configuration. Inhibition of this enzyme by (S)‐4‐aminohex‐5‐ynoic acid involves the abstraction
M, Bouclier, M J, Jung, B, Lippert
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Porphyrins and porphyrinogen carboxy-lyase in hexachlorobenzene-induced porphyria [PDF]
Biochemical Journal, 1977 1. Qualitative and quantitative studies of the porphyrins and the porphyrinogen carboxylyase of the liver, spleen, kidney, harderian gland and erythrocytes from normal rats and from those hexachlorobenzene-induced porphyria were carried out. 2. Hexachlorobenzene has no effect on erythrocyte porphyrin content, but produces a decrease in that of ...
L C, San Martín De Viale +3 more
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, 2017 The basic natural amino acid L-argininosuccinate containing two chiral centers occurs in L-alanine, L-arginine, L-aspartate, L-glutamate and L-proline metabolic pathways and plays a role in the biosynthesis of secondary metabolites and other amino acids.
B. Schoenenberger +5 more
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The Pectin Lyases in Arabidopsis thaliana: Evolution, Selection and Expression Profiles
PLoS ONE, 2012 Pectin lyases are a group of enzymes that are thought to contribute to many biological processes, such as the degradation of pectin. However, until this study, no comprehensive study incorporating phylogeny, chromosomal location, gene duplication, gene ...
Jun Cao
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