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N-acetyllactosamine synthase is a galactosyltransferase enzyme. It is a component of lactose synthase This enzyme modifies the connection between two molecule UDP-galactose and N-actyl-D-glucosamine and generates two different molecules UDP and N-acetyllactosamine as products. The main function of the enzyme is associated with the biosynthesis of glycoproteins and glycolipids in both human and animals. In human, the activity of this enzyme can be found in Golgi apparatus.
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In enzymology, a methylenetetrahydrofolate dehydrogenase (NADP+) (EC 1.5.1.5) is an enzyme that catalyzes the chemical reaction
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In enzymology, a 3-mercaptopyruvate sulfurtransferase is an enzyme that catalyzes the chemical reactions of 3-mercaptopyruvate. This enzyme belongs to the family of transferases, specifically the sulfurtransferases. This enzyme participates in cysteine metabolism. It is encoded by the MPST gene.
The enzyme 3-dehydroquinate dehydratase (EC 4.2.1.10) catalyzes the chemical reaction
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Morpheeins are proteins that can form two or more different homo-oligomers, but must come apart and change shape to convert between forms. The alternate shape may reassemble to a different oligomer. The shape of the subunit dictates which oligomer is formed. Each oligomer has a finite number of subunits (stoichiometry). Morpheeins can interconvert between forms under physiological conditions and can exist as an equilibrium of different oligomers. These oligomers are physiologically relevant and are not misfolded protein; this distinguishes morpheeins from prions and amyloid. The different oligomers have distinct functionality. Interconversion of morpheein forms can be a structural basis for allosteric regulation, an idea noted many years ago, and later revived. A mutation that shifts the normal equilibrium of morpheein forms can serve as the basis for a conformational disease. Features of morpheeins can be exploited for drug discovery. The dice image represents a morpheein equilibrium containing two different monomeric shapes that dictate assembly to a tetramer or a pentamer. The one protein that is established to function as a morpheein is porphobilinogen synthase, though there are suggestions throughout the literature that other proteins may function as morpheeins.
References
- ↑ Stipanuk MH, Ueki I, Dominy JE, Simmons CR, Hirschberger LL (May 2009). "Cysteine dioxygenase: a robust system for regulation of cellular cysteine levels". Amino Acids. 37 (1): 55–63. doi:10.1007/s00726-008-0202-y. PMC 2736881 . PMID 19011731.
- ↑ Roychaudhuri R (March 2023). "Mammalian D-Cysteine: A new addition to the growing family of biologically relevant D-amino acids". Chirality: chir.23555. doi:10.1002/chir.23555. PMID 36890664. S2CID 257426578.
- ↑ Tolosa EA, Chepurnova NK, Khomutov RM, Severin ES (February 1969). "Reactions catalysed by cysteine lyase from the yolk sac of chicken embryo". Biochimica et Biophysica Acta (BBA) - Enzymology. 171 (2): 369–371. doi:10.1016/0005-2744(69)90174-0. PMID 5813025.
- 1 2 Sun Q, Collins R, Huang S, Holmberg-Schiavone L, Anand GS, Tan CH, et al. (January 2009). "Structural basis for the inhibition mechanism of human cystathionine gamma-lyase, an enzyme responsible for the production of H(2)S". The Journal of Biological Chemistry. 284 (5): 3076–3085. doi: 10.1074/jbc.M805459200 . PMID 19019829.
- ↑ Mccorquodale DJ (December 1964). "The separation and partial purification of aminoacyl-RNA synthetases from Escherichia coli". Biochimica et Biophysica Acta (BBA) - Specialized Section on Nucleic Acids and Related Subjects. 91 (4): 541–548. doi:10.1016/0926-6550(64)90001-5. PMID 14262440.
- ↑ Maresca B, Jacobson E, Medoff G, Kobayashi G (September 1978). "Cystine reductase in the dimorphic fungus Histoplasma capsulatum". Journal of Bacteriology. 135 (3): 987–992. doi:10.1128/jb.135.3.987-992.1978. PMC 222474 . PMID 211119.
- 1 2 Hipólito A, Nunes SC, Vicente JB, Serpa J (September 2020). "Cysteine Aminotransferase (CAT): A Pivotal Sponsor in Metabolic Remodeling and an Ally of 3-Mercaptopyruvate Sulfurtransferase (MST) in Cancer". Molecules. 25 (17): 3984. doi: 10.3390/molecules25173984 . PMC 7504796 . PMID 32882966.
- ↑ Chen Y, Shertzer HG, Schneider SN, Nebert DW, Dalton TP (October 2005). "Glutamate cysteine ligase catalysis: dependence on ATP and modifier subunit for regulation of tissue glutathione levels". The Journal of Biological Chemistry. 280 (40): 33766–33774. doi: 10.1074/jbc.M504604200 . PMID 16081425.
- ↑ Kredich NM, Becker MA, Tomkins GM (May 1969). "Purification and characterization of cysteine synthetase, a bifunctional protein complex, from Salmonella typhimurium". The Journal of Biological Chemistry. 244 (9): 2428–2439. doi: 10.1016/S0021-9258(19)78241-6 . PMID 4977445.
- ↑ Nagai S, Black S (April 1968). "A thiol-disulfide transhydrogenase from yeast". The Journal of Biological Chemistry. 243 (8): 1942–1947. doi: 10.1016/S0021-9258(18)93532-5 . PMID 5646485.