D-amino acid dehydrogenase

D-amino-acid dehydrogenase (EC 1.4.99.1) is a bacterial enzyme that catalyses the oxidation of D-amino acids into their corresponding oxoacids. It contains both flavin and nonheme iron as cofactors.[1] The enzyme has a very broad specificity and can act on most D-amino acids.[2]

D-amino acid + H2O + acceptor <=> a 2-oxo acid + NH3 + reduced acceptor

This reaction is distinct from the oxidation reaction catalysed by D-amino acid oxidase that uses oxygen as a second substrate, as the dehydrogenase can use many different compounds as electron acceptors, with the physiological substrate being coenzyme Q.[1][3]

D-amino acid dehydrogenase is an enzyme that catalyzes NADPH from NADP+ and D- glucose to produce D- amino acids and glucose dehydrogenase. Some but not limited to these amino acids are D-leucine, D-isoleucine, and D-Valine, which are essential amino acids that humans cannot synthesize due to the fact that they are not included in their diet. Moreover, D- amino acids catalyzes the formation of 2-oxo acids to produce D- amino acids in the presence of DCIP which is an electron acceptor.[4]

Additionally, D- amino acid dehydrogenase is used in Dye-Linked dehydrogenase (Dye-DHs) which uses artificial dyes such as 2,6-Dichloroindophenol (DCIP) as their electron acceptor rather than using their natural electron acceptors. This can accelerate the reaction between the enzyme and the substrate when the electrons are being transferred. [5]

See also

References
  1. Olsiewski PJ, Kaczorowski GJ, Walsh C (25 May 1980). "Purification and properties of D-amino acid dehydrogenase, an inducible membrane-bound iron-sulfur flavoenzyme from Escherichia coli B". J. Biol. Chem. 255 (10): 4487–94. PMID 6102989.
  2. Tsukada K (10 October 1966). "D-amino acid dehydrogenases of Pseudomonas fluorescens". J. Biol. Chem. 241 (19): 4522–8. PMID 5925166.
  3. Jones H, Venables WA (1983). "Effects of solubilisation on some properties of the membrane-bound respiratory enzyme D-amino acid dehydrogenase of Escherichia coli". FEBS Lett. 151 (2): 189–92. doi:10.1016/0014-5793(83)80066-0. PMID 6131836.
  4. Akita, Hironaga; Suzuki, Hirokazu; Doi, Katsumi; Ohshima, Toshihisa (1 February 2014). "Efficient synthesis of d-branched-chain amino acids and their labeled compounds with stable isotopes using d-amino acid dehydrogenase". Applied Microbiology and Biotechnology. 98 (3): 1135–1143. doi:10.1007/s00253-013-4902-1. ISSN 1432-0614. PMID 23661083.
  5. Satomura, Takenori; Sakuraba, Haruhiko; Suye, Shin-ichiro; Ohshima, Toshihisa (1 November 2015). "Dye-linked D-amino acid dehydrogenases: biochemical characteristics and applications in biotechnology". Applied Microbiology and Biotechnology. 99 (22): 9337–9347. doi:10.1007/s00253-015-6944-z. ISSN 1432-0614. PMID 26362681.


This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.