Explore chapters and articles related to this topic
Biology of microbes
Published in Philip A. Geis, Cosmetic Microbiology, 2006
Other more common mechanisms for assimilating nitrogen are ammonia incorporation and assimilatory nitrate reduction. Ammonia is easily incorporated into amino acids by forming the alanine amino acid directly by amination of pyruvate using the alanine dehydrogenase enzyme. Alternatively, a cell can form glutamate (an amino acid) by aminating α-ketoglutarate (a TCA cycle intermediate) using the glutamate dehydrogenase enzyme. Once these two amino acids have been formed, the ammonia they carry (now called an α-amino group) can be transferred to other carbon skeletons of other catabolic intermediates by transamination to form several other amino acids.
Glutamate Dehydrogenase
Published in Elling Kvamme, Glutamine and Glutamate in Mammals, 1988
Gel-filtration,173 fluorescence titration,174 and cross-linking175 experiments have shown glutamate dehydrogenase to be capable of complexing with aspartate aminotransferase (EC 2.6.1.1.). The complex formed was shown to possess aspartate dehydrogenase activity. A similar complex formed with alanine aminotransferase (EC 2.6.1.2.) was found to possess increased alanine dehydrogenase activity;173 ADP and GTP were shown to affect the aspartate dehydrogenase activity of mixtures of aspartate aminotransferase and glutamate dehydrogenase, probably by affecting the the self-association of glutamate dehydrogenase and thus regulating the amount of disaggregated glutamate dehydrogenase available for interaction with the aminotransferase.173 The concentrations of these two enzymes in liver and brain mitochondria were estimated to be higher than the dissociation constant for their complex.173 However, since aggregated forms of glutamate dehydrogenase did not appear to interact with the aminotransferase, competition between these processes, and perhaps membrane binding as well, would be expected to occur and the physiological significance of the process remains unclear.
Biocatalysts: The Different Classes and Applications for Synthesis of APIs
Published in Peter Grunwald, Pharmaceutical Biocatalysis, 2019
Transaminases (or aminotransferases) are enzymes transferring an amino group (EC 2.6.1.-). In the recent past, the use of PLP-dependent ω-transaminases (ω-TA; meanwhile (R)- and (S)-selective ω-TAs are known) for the synthesis of optically pure amines gained increasing interest in connection with the synthesis of active pharmaceutical ingredients (for reviews see, e.g., Fuchs et al., 2015; Simon et al., 2014). ω-TAs catalyze the reversible amination/deamination of suited substrates to yield optically pure amines either by kinetic resolution (one amine enantiomer is converted into a ketone whereas the desired amine enantiomer is left behind) or by asymmetric synthesis starting from a prochiral ketone. In these cases, the amine donor is l-alanine that is converted to pyruvate. In order to shift the equilibrium to the product side, the keto acid is converted to lactate in presence of lactate dehydrogenase; pyruvate decarboxylase has also been used for this purpose. Alternatively pyruvate may be recycled to alanine in presence of a alanine dehydrogenase. Very promising is the recently described use of o-xylylenediamine as a low-cost non-chiral amine donor (Green et al., 2014); in addition, spontaneous polymerization of the aromaticisoindoleformed during the course of the reaction yields intensively colored derivatives which may serve as a high-throughput screening platform to identify ω-TA activities. These enzymes work not only in an aqueous buffer solution but also in organic solvents.
Is interleukin-2 an optimal marker for diagnosing tuberculosis infection? A systematic review and meta-analysis
Published in Annals of Medicine, 2020
Xia Qiu, Huiqing Wang, Ying Tang, Xiaojuan Su, Long Ge, Yi Qu, Dezhi Mu
The main characteristics of the 18 articlesare listed in Table 1 [23–40]. In total, 1404 participants (ATB patients: 373; LTBI individuals: 542; non-TB controls: 489) were involved. These studies, came from 10 countries, ranged from 2008 to 2018. The LTBI populations mostly included household contacts, healthcare workers and close contacts. Positive Mtb culture and/or sputum smear microscopy were the gold standards for ATB. The IGRA and/or TST were as the reference standards for LTBI individuals. The cut-offs of IL-2 ranged from 10.7 to 976.3 pg/ml or 12.5 to 275 spot-forming cells per million peripheral blood mononuclear cells. IL-2 were reported by Mtb-specific antigen stimulated, and the specific antigens included early secreted antigenic target-6 (ESAT-6), culture filtrate protein-10 (CFP-10), TB7.7, L-alanine dehydrogenase (Ala-DH) and purified protein derivative (PPD). Only one article reported that the populations were co-infected with HIV. Other baseline characteristics (gender, age and migrants) are shown in Supplementary Table 1.
A patient-oriented approach to long-term use of omalizumab in chronic spontaneous urticaria
Published in Cutaneous and Ocular Toxicology, 2021
The laboratory findings consisting of liver and renal function tests and full blood count were in normal ranges both before and after omalizumab treatment. The statistical difference was found only between aspartate dehidrogenase (AST) levels (p = 0.019) which the levels after omalizumab treatment were slightly increased but still in normal ranges. There was no statistical difference between haemoglobin, leukocyte, platelet counts, blood urea nitrogen, creatinine, and alanine dehydrogenase (ALT) levels before and after treatment (p > 0.05).