Part:BBa_K4929000

FAD

Basic Part - BBa_K4929000 (FAD)

Profile

• Name: FAD
• Base Pairs: 2119 bp
• Origin: Yeast, Synthetic
• Properties: Catalyses the oxidation of histamine to produce indole acetaldehyde and ammonia ions and is known as histamine dehydrogenase.

Usage and Biology

Amine Dehydrogenase (AmDH), most of which use Tryptophan Tryptophylquinone (TTQ) as a cofactor, can oxidize amines to dehydrogenate to produce the corresponding aldehydes and ammonia, and the electrons generated by its oxidation of primary amines are passed from TTQ through Cu2+ on the copper-containing protein cofactor to the final electron receptor [1]. Methylamine Dehydrogenase (MADH) was the first enzyme discovered to use TTQ as a cofactor, and the electrons generated from the oxidation of methylamine are passed from TTQ to the electron acceptor cytochrome c via amicyanin [2].

In addition to amine dehydrogenases with TTQ as a cofactor, there also exist amine dehydrogenases that do not have TTQ as a cofactor and contain a covalently bound 6-S-cysteinyl flavin mononucleotide (6-S-Cys-FMN) and a [4Fe-4S] cluster as a redox cofactor that catalyzes the oxidation of histamine to produce indole acetaldehyde and ammonia ions, hence the name histamine dehydrogenase [3].

Gene Map of FAD

Most of these enzymes contain two subunits, such as histamine dehydrogenase (MSMADH) in Nocardioides simplex, a homodimeric protein that oxidizes mainly histamine, but also oxidizes putrescine, but catalyzes putrescine with only 0.7% of the efficiency of histamine [3]. Histamine dehydrogenase (HDH-R) from Rhizobium sp. is also a homodimer, and its optimal substrate is histamine; it shows the highest enzyme activity at pH 9.0 and 70 °C, and is considered to be the most histamine-specific of the amine oxidases and amine dehydrogenases [4]. There are also a small number of such enzymes that contain more than two subunits, such as histamine dehydrogenase (HADH) from the halophilic archaeon Natrinema gari, which is a heterotrimer, and the enzyme was found to be active at pH 6.5-8.5, 40-60 °C under high-salt conditions (3.5-5.0 mol/L NaCl) with high solubility and catalytic activity [5]. In addition, 3-phosphoglyceraldehyde dehydrogenase from L. plantarum SGJ-24 can also degrade histamine, and its optimal reaction pH and temperature were 7.5 and 40 °C, respectively, and it was able to stabilize at conditions lower than 55 °C and pH 6.5-8.5, and its degradation rate of histamine could reach 52.2% [6]. It has been confirmed that amine dehydrogenase is an alkaline oxidase with an optimal reaction pH in the range of 7.5-9.0, which cannot play an effective role in amine degradation in acidic fermented foods, and the enzyme activity is susceptible to strong inhibition by carbonyl reagents, such as amino ureas and aminoguanidine, and thus is not suitable for the degradation of biogenic amines in fermented foods [6-7].

References:

1. Yukl ET, Davidson VL. Diversity of structures, catalytic mechanisms, and processes of cofactor biosynthesis of tryptophylquinone-bearing enzymes. Archives of Biochemistry and Biophysics, 2018, 654: 40-46. DOI:10.1016/j.abb.2018.07.012.
2. Chen LY, Durley R, Poliks BJ, Hamada K, Chen ZW, Mathews FS, Davidson VL, Satow Y, Huizinga E, Vellieux FMD, et al. Crystal structure of an electron-transfer complex between methylamine dehydrogenase and amicyanin. Biochemistry, 1992, 31(21): 4959-4964. DOI:10.1021/bi00136a006.
3. Limburg J, Mure M, Klinman JP. Cloning and characterization of histamine dehydrogenase from Nocardioides simplex. Archives of Biochemistry and Biophysics, 2005, 436(1): 8-22. DOI:10.1016/j.abb.2004.11.024.
4. Bakke M, Sato T, Ichikawa K, Nishimura I. Histamine dehydrogenase from Rhizobium sp.: gene cloning, expression in Escherichia coli, characterization and application to histamine determination. Journal of Biotechnology, 2005, 119(3): 260-271. DOI:10.1016/j.jbiotec.2005.04.005.
5. Zhou DW, Visessanguan W, Chaikaew S, Benjakul S, Oda K, Wlodawer A. Crystallization and preliminary crystallographic analysis of histamine dehydrogenase from Natrinema gari BCC 24369. Acta Crystallographica Section F, Structural Biology Communications, 2014, 70: 942-945. DOI:10.1107/S2053230X14011327
6. Zhang QF. Purification and characterization of an enzyme capable of histamine degradation from Lactobacillus plantarum[D]. Yantai: Master's Thesis of Yantai University, 2018 (in Chinese).
7. Lee YC, Lin CS, Liu FL, Huang TC, Tsai YH. Degradation of histamine by Bacillus polymyxa isolated from salted fish products. Journal of Food and Drug Analysis, 2015, 23(4): 836-844. DOI:10.1016/j.jfda.2015.02.003.

Sequence and Features

Assembly Compatibility:

• 10
  COMPATIBLE WITH RFC[10]
• 12
  INCOMPATIBLE WITH RFC[12]

  Illegal NotI site found at 1968
  
• 21
  INCOMPATIBLE WITH RFC[21]

  Illegal BamHI site found at 1315
  Illegal BamHI site found at 1705
  Illegal XhoI site found at 625
  Illegal XhoI site found at 1014
  Illegal XhoI site found at 1154
  Illegal XhoI site found at 1200
  
• 23
  COMPATIBLE WITH RFC[23]
• 25
  INCOMPATIBLE WITH RFC[25]

  Illegal NgoMIV site found at 439
  Illegal NgoMIV site found at 1185
  Illegal NgoMIV site found at 1908
  Illegal NgoMIV site found at 2018
  Illegal AgeI site found at 33
  Illegal AgeI site found at 48
  Illegal AgeI site found at 566
  Illegal AgeI site found at 1990
  
• 1000
  INCOMPATIBLE WITH RFC[1000]

  Illegal BsaI.rc site found at 352
  Illegal SapI site found at 1570