Results 1 to 10 of about 2,626 (154)
Unveiling the Potential of Lentilactobacillus hilgardii in Malolactic Fermentation: Comparative Genomics and Fermentation Dynamics. [PDF]
This 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
Functional and structural characterization of Stenotrophomonas maltophilia EntB, an unusual form of isochorismatase for siderophore synthesis. [PDF]
The crystal structure of S. maltophilia EntB revealed an unusual form of isochorismate lyase that is involved in siderophore biosynthesis.Clinical and environmental isolates of Stenotrophomonas maltophilia produce an enterobactin‐like siderophore that promotes bacterial growth under low‐iron conditions.
Nas MY +6 more
europepmc +2 more sources
La L-glutamate-1-carboxy-lyase des Pervenches indigènes [PDF]
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
Classificação do diabete melito Diabetes mellitus classification
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
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
openaire +2 more sources
UDP-glucuronate carboxy-lyase in cultured chondrocytes.
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
openaire +2 more sources
Porphyrin biosynthesis. VII. Porphyrinogen carboxy-lyase from avian erythrocytes. Purification and properties [PDF]
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
Effects of Certain Hydroxamic Acids on L-Glutamate 1-Carboxy-lyase
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
openaire +2 more sources
Expression of the LEA‐K peptide in E. coli BL21 (DE3) improved bacterial viability under acidic stress (pH4), suggesting a protective function. RNA‐sequencing of LEA‐K‐expressing vs. non‐expressing cells revealed 283 differentially expressed genes (DEGs). In silico docking linked LEA‐K to two‐component systems (TCS) proteins (Rcs, BtsS/R, and EnvZ/OmpR)
Khaled Metwally, Shinya Ikeno
wiley +1 more source
Characterization of anhydromevalonate phosphate decarboxylase, the UbiD‐family decarboxylase involved in the archaeal mevalonate pathway, was conducted. The enzyme is responsible for the biosynthesis of isoprenoids, such as archaeal membrane lipids, respiratory quinones, and dolichols.
Rino Ishikawa +9 more
wiley +1 more source

