328-42-7Relevant articles and documents
Oxalacetic acid as amino group acceptor in transamination.
CAMMARATA,COHEN
, p. 117 - 120 (1953)
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Structure Elucidation of Phomopsin A, a Novel Cyclic Hexapeptide Mycotoxin produced by Phomopsis leptostromiformis
Culvenor, Claude C. J.,Cockrum, Peter A.,Edgar, John A.,Frahn, John L.,Gorst-Allman, Charles P.,et al.
, p. 1259 - 1262 (1983)
Phomopsin A, the main mycotoxin isolated from cultures of Phomopsis leptostromiformis and the cause of lupinosis disease in animals grazing infected lupins, is a cyclic hexapeptide containing 3-hydroxyisoleucine, 3,4-didehydrovaline, N-methyl-3-(3-chloro-4,5-dihydroxyphenyl)-3-hydroxyalanine, E-2,3-didehydroaspartic acid, E-2,3-didehydroisoleucine, and 3,4-didehydroproline; its 13C n.m.r. spectrum was completely assigned and the amino-acid sequence established unambiguously by extensive heteronuclear 13C- selective population inversion n.m.r. experiments.
Oxaloacetic acid formation in liver mitochondria and its influence on succinate oxidation with the addition of ethylenediaminetetraacetic acid.
KUNZ,MUELLER,STRACK
, p. 204 - 211 (1960)
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Kritzmann
, p. 603 (1939)
Bacterial flavoprotein monooxygenase YxeK salvages toxic S-(2-succino)-adducts via oxygenolytic C–S bond cleavage
Ellis, Holly R.,Kammerer, Bernd,Lagies, Simon,Matthews, Arne,Sch?nfelder, Julia,Schleicher, Erik,Stull, Frederick,Teufel, Robin
, (2021/10/06)
Thiol-containing nucleophiles such as cysteine react spontaneously with the citric acid cycle intermediate fumarate to form S-(2-succino)-adducts. In Bacillus subtilis, a salvaging pathway encoded by the yxe operon has recently been identified for the detoxification and exploitation of these compounds as sulfur sources. This route involves acetylation of S-(2-succino)cysteine to N-acetyl-2-succinocysteine, which is presumably converted to oxaloacetate and N-acetylcysteine, before a final deacetylation step affords cysteine. The critical oxidative cleavage of the C–S bond of N-acetyl-S-(2-succino)cysteine was proposed to depend on the predicted flavoprotein monooxygenase YxeK. Here, we characterize YxeK and verify its role in S-(2-succino)-adduct detoxification and sulfur metabolism. Detailed biochemical and mechanistic investigation of YxeK including 18O-isotope-labeling experiments, homology modeling, substrate specificity tests, site-directed mutagenesis, and (pre-)steady-state kinetics provides insight into the enzyme’s mechanism of action, which may involve a noncanonical flavin-N5-peroxide species for C–S bond oxygenolysis.
Two-Dimensional Tin Selenide (SnSe) Nanosheets Capable of Mimicking Key Dehydrogenases in Cellular Metabolism
Gao, Meng,Wang, Zhenzhen,Zheng, Huizhen,Wang, Li,Xu, Shujuan,Liu, Xi,Li, Wei,Pan, Yanxia,Wang, Weili,Cai, Xiaoming,Wu, Ren'an,Gao, Xingfa,Li, Ruibin
supporting information, p. 3618 - 3623 (2020/02/13)
While dehydrogenases play crucial roles in tricarboxylic acid (TCA) cycle of cell metabolism, which are extensively explored for biomedical and chemical engineering uses, it is a big challenge to overcome the shortcomings (low stability and high costs) of recombinant dehydrogenases. Herein, it is shown that two-dimensional (2D) SnSe is capable of mimicking native dehydrogenases to efficiently catalyze hydrogen transfer from 1-(R)-2-(R′)-ethanol groups. In contrary to susceptible native dehydrogenases, lactic dehydrogenase (LDH) for instance, SnSe is extremely tolerant to reaction condition changes (pH, temperature, and organic solvents) and displays extraordinary reusable capability. Structure–activity analysis indicates that the single-atom structure, Sn vacancy, and hydrogen binding affinity of SnSe may be responsible for their catalytic activity. Overall, this is the first report of a 2D SnSe nanozyme to mimic key dehydrogenases in cell metabolism.