Results 1 to 10 of about 2,651 (134)
Unveiling the Potential of Lentilactobacillus hilgardii in Malolactic Fermentation: Comparative Genomics and Fermentation Dynamics. [PDF]
Microb BiotechnolThis study explores the metabolic potential of Lentilactobacillus hilgardii for malolactic fermentation in winemaking. Genomic and in silico analyses, combined with experimental validation, reveal its resilience at low temperatures and unique enzymatic traits. Comparative insights with Oenococcus oeni highlight L.
Mantegazza G +5 more
europepmc +2 more sources
Classificação do diabete melito Diabetes mellitus classification
Arquivos Brasileiros de Cardiologia, 2010 A correta classificação do diabete melito (DM) permite o tratamento mais adequado e compreende quatro categorias: DM tipo 1; DM tipo 2; Outros tipos e Diabete Gestacional.
Jorge de Faria Maraschin +3 more
doaj +1 more source
Inhibition of Glutamic Acid Carboxy-Lyase by Alanosine
Experimental Biology and Medicine, 1968 SummaryAlanosine is an inhibitor of glutamic acid carboxy-lyase (C-L) of bacterial origin, but not of those from squash and rat brain. Its action is competitive in respect to glutamic acid, but noncompetitive in respect to pyridoxal phosphate. Other bacterial amino acid C-L's tested, while sensitive to hydroxylamine, are not inhibited by alanosine.
G R, Gale, L M, Atkins
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UDP-glucuronate carboxy-lyase in cultured chondrocytes.
Journal of Biological Chemistry, 1977 UDP-glucuronate carboxy-lyase has been demonstrated in chick chondrocytes in tissue culture. It occurs in the particulate fraction, and its activity is stimulated by exogenous NAD. The enzyme is allosterically activated by UDP-glucuronate and inhibited by UDP-xylose, n Values of 2.8 indicate positive cooperativity of at least three interacting sites on
K V, John, N B, Schwartz, H, Ankel
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La L-glutamate-1-carboxy-lyase des Pervenches indigènes [PDF]
Bulletin de la Société Botanique de France, 1975 ResumeLes variations de l'acide glutamique et de l'acide γ;-aminobutyrique libres au cours de la vegetation ne sont pas directement superposables a celles de l'activite de la glutamate decarboxylase. Ces dernieres sont dues aux variations de la synthese de l'enzyme.
Pierre Cillard +2 more
openaire +1 more source
Porphyrin biosynthesis. VII. Porphyrinogen carboxy-lyase from avian erythrocytes. Purification and properties [PDF]
Biochimica et Biophysica Acta (BBA) - Enzymology, 1970 1. Uroporphyrinogen carboxy-lyase (EC 4.1.1.d), the enzyme catalysing the decaroxylation of uroporphyrinogen to coproporphyrinogen, has been isolated from normal chicken erythrocytes. The enzyme was purified 220-fold with a yield of 24% from haemolysate supernatant by DEAE-cellulose batch treatment, (NH4)2SO4 fractionation and chromatography on DEAE ...
Tomio, J.M. +3 more
openaire +4 more sources
Unlocking a Nitrosuccinate Lyase for Decarboxylative Enzymatic Hydronitration
Angewandte Chemie, EarlyView.The nitrosuccinate lyase CreD catalyzes C–NO2 bond formation using nitrite in water and shows synthetic practicality with high turnover numbers up to 102,000. A combination of protein engineering and computational methods helped to reveal the mechanistic principles that underpin this unique enzymatic activity.
Matteo Aleotti +9 more
wiley +2 more sources
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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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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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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