Distribution and Biological Functions of Pyruvate Carboxylase in Nature
D. B. Keech, J. C. Wallace in Pyruvate Carboxylase, 2018
It was at first thought902 that the occurrence of either pyruvate carboxylase or PEP carboxylase was mutually exclusive of the other. However, these two enzymes have now been reported in Azotobacter vinelandii;502,758Pseudomonas fluorescens,404Ps. citronellolis,612Brevibacterium lacto term en turn,885Thiobacillus novellus,542 and some of the Chromatiaceae.719,999 Among the Chromatiaceae, Sahl and Truper719 found considerable variation between species as to whether both pyruvate carboxylase and PEP carboxylase occurred together and in the way their activities were affected by the growth conditions.
Factors Controlling the Microflora of the Skin
Michael J. Hill, Philip D. Marsh in Human Microbial Ecology, 2020
Until relatively recently there was a belief that only one genus of coryneform (Corynebacterium) was present on human skin; this belief hampered attempts to devise taxonomic schemes for the coryneforms. We now know that representatives of the genera Brevibacterium, Corynebacterium, and Propionibacterium are the major coryneforms with contributions from other genera which are at present hard to assess. Coryneforms are separated principally on the composition of their cell walls. Brevibacterium species possess meso-diaminopimelic acid (DAP) and galactose as the major sugar but lack characteristic lipids known as mycolic acids. Corynebacterium species also possess meso-DAP but in addition have an arabinogalactan and relatively small mycolic acids (Rhodococcus C24–36 is distinguished from Corynebacterium C24–30 chiefly by its slightly longer mycolic acids) while Propionibacterium species possess LL-DAP and glucose, lack mycolic acids, and are best grown under anaerobic conditions, despite being facultative aerobes.
Linezolid
M. Lindsay Grayson, Sara E. Cosgrove, Suzanne M. Crowe, M. Lindsay Grayson, William Hope, James S. McCarthy, John Mills, Johan W. Mouton, David L. Paterson in Kucers’ The Use of Antibiotics, 2017
Linezolid has good activity against a wide range of corynebacteria, including antibiotic-resistant strains and clinical isolates (Fernandez-Roblas et al., 2009; Nhan et al., 2012; Cacopardo et al., 2013), Corynebacterium diphtheriae (nontoxigenic isolates tested) (Zasada et al., 2010), and other coryneforms such as Arthrobacter spp., Brevibacterium spp., Dermabacter hominis, Microbacterium spp., and Turicella otitidis; it is also active against Rhodococcus equi (Jones et al., 1996; Bowersock et al., 2000; Goldstein et al., 2003a, 2003b; Funke and Nietznik, 2005; Jones et al., 2007c).
Changes in the fecal bacterial microbiota associated with disease severity in alcoholic hepatitis patients
Published in Gut Microbes, 2020
Sonja Lang, Bradley Fairfied, Bei Gao, Yi Duan, Xinlian Zhang, Derrick E. Fouts, Bernd Schnabl
Llopis et al. used a histologic scoring system (alcoholic hepatitis score) to determine alcoholic hepatitis severity and also identified an expansion of Streptococci, as well as Bifidobacteria, and Enterobacteria in patients with severe disease. Streptococci and Enterobacteria were both positively correlated with the alcoholic hepatitis score, and Enterobacteria was also positively correlated with serum bilirubin level.7 Lastly, Puri et al. examined the circulating microbiome in patients with alcoholic hepatitis with severity determined by MELD greater than 20. They noted an expansion of Brevibacterium and Staphylococcus in the circulating microbiome of alcoholic hepatitis patients with severe disease compared to moderate disease. Regression analysis including all alcohol-consuming patients found a negative correlation between MELD score and Janthinobacterium and Enhydrobacter, two genera of the Proteobacteria phylum.18 We did not see these associations in our analyses, though it is important to note that the study by Puri et al. uses 16S rRNA gene sequencing from whole blood samples.
Recent approaches to ameliorate selectivity and sensitivity of enzyme based cholesterol biosensors: a review
Published in Artificial Cells, Nanomedicine, and Biotechnology, 2018
Anjum Gahlaut, Vinita Hooda, Vikas Dhull, Vikas Hooda
Cholesterol biosensors contain cholesterol oxidase (ChO) and cholesterol esterase (ChE) as recognition element. Cholesterol oxidase is a flavoenzyme which uses flavin adenine dinucleotide (FAD) as cofactor and catalyses the oxidation and isomerisation of steroids containing a hydroxyl group at 3’ position. ChO exists as monomer with molecular mass 55 kDa. ChO is commonly obtained from Streptomyces hygroscopicus and Brevibacterium sterolicum. ChO obtained from Streptomyces hygroscopicus is more sensitive and show linearity up to 20.7 mmol/L. It’s another benefit is that it does not show interference due to the presence of hemoglobin [17]. Cholesterol oxidase belongs to flavin-specific oxidoreductases family. Its prosthetic group FAD is covalently attached to the core protein in Streptomyces and is non-covalently bound to the core enzyme in Brevibacterium [18]. Cholesterol esterase catalyses the hydrolysis of sterol esters into sterols and fatty acids. ChE is found in pancreas in bulk quantity, but it has been detected in other tissues also. It exists in polymeric form [19]. While determining cholesterol concentration in a given sample cholesterol esterase first hydrolyses esterified cholesterol and then cholesterol oxidase oxidizes cholesterol to produces cholest-4-en-3-one and hydrogen peroxide (H2O2). In amperometric biosensors electric potential is applied on H2O2 which get oxidized to produce electrons and the flow of electrons produces current. The current produced is directly proportional to the concentration of cholesterol present in the sample. Concentration of released protons is measured by potentiometric biosensor.
Preclinical developments of enzyme-loaded red blood cells
Published in Expert Opinion on Drug Delivery, 2021
Luigia Rossi, Francesca Pierigè, Alessandro Bregalda, Mauro Magnani
However, it is noteworthy that MGL from P. putida, a parasitic and potentially pathogenic microorganism, possesses the ability to partially catabolize L-cysteine [46]; hence, it would be desirable to carry on preclinical studies where a MGL from safer origin than P. putida and with a different specificity can be loaded inside RBCs to preserve cysteine plasma levels. MGL-BL929 from Brevibacterium aurantiacum [47], a safe microorganism abundantly present in food, could be a possible candidate to this extend.
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