Part:BBa_K4929002

AocI

Basic Part - BBa_K4929002 (AocI)

Profile

• Name: AocI
• Base Pairs: 2285 bp
• Origin: Yeast, Synthetic
• Properties: This gene encodes a metal-binding membrane glycoprotein that oxidatively deaminates putrescine, histamine, and related compounds.

Usage and Biology

This gene encodes a metal-binding membrane glycoprotein that oxidatively deaminates putrescine, histamine, and related compounds. The encoded protein is inhibited by amiloride, a diuretic that acts by closing epithelial sodium ion channels. Alternatively, spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Jan 2013]

Figure 1. Gene Map of AocI.

Amine oxidases (AOs) catalyze the oxidation of biogenic amines to form aldehydes, ammonia, and hydrogen peroxide. AOs were first discovered by Yamada et al [1], where fungi formed AOs in mycelium when grown with mono- or diamines as nitrogen sources, whereas other nitrogen sources did not have any effect on enzyme formation. Certain microorganisms can secrete amine oxidase, which reduces the biogenic amine content in fermented foods; meanwhile, biogenic amine oxidase, which can degrade biogenic amines, also exists in the human gut and is used to regulate intracellular amine content, maintain intra- and extracellular acid-base balance, and safeguard human health [2]. The classification of AOs mainly depends on their molecular structures, amino acid sequences, and cofactor structures. Currently, amine oxidases of microbial origin are found to be mainly flavin-containing amine oxidases (EC 1.4.3.4) and copper-containing amine oxidases (EC 1.4.3.6).

Copper amine oxidases (CuAOs) are a class of copper-containing reductases, and such enzymes contain two types of cofactors: 2,4,5-dihydroxyphenylalanine quinone (TPQ) and lysine tyrosine quinone (LTQ) that are produced post-translationally from specific tyrosine residues [3]. CuAOs are present in Escherichia coli, Arthrobacter globigii, Hansenula polymorphica Arthrobacter sphaericus, Hansenula polymorphica, and Picrosporum, and the amine oxidase from Arthrobacter sphaericus KAIT-B-007 was purified twice on a dextran gel S-200 [4]. The specific activity of amine oxidase from Arthrobacter sphaericus KAIT-B-007 was 14.3 U/mg. The enzyme has good heat resistance, and the enzyme activity remained stable at 65°C, and the residual enzyme activity was 91% after 10 min at 70°C [5]. The copper-containing oxidase 2 from Arthrobacter taurus TC-1 showed high catalytic efficiency for phenylethylamine, tyramine and histamine, and the relative value of Kcat/Km was 100:49.6:7.6 [6]; Hansenula polymorpha H525 contains a copper amine oxidase gene, and the crude enzyme solution was added to grape juice containing biogenic amines for 7 d, the content of phenylethylamine and tyramine was reduced to almost zero [4].

References:

1. Yamada H， Adachi O， Ogata K. Amine oxidases of microorganisms: part I. Formation of amine oxidase by fungi. Agricultural and biological chemistry，1965，29(2): 117-123. 49.
2. Song Y, Dong Q. Research progress in formation and control of the biogenic amine in Chinese rice wine [J]. Science and Technology of Food Industry, 2016, 37(8): 387-391.
3. Li B B， Lu S L. The importance of amine-degrading enzymes on the biogenic amine degradation in fermented foods: a review[J]. Process Biochemistry，2020，99: 331-339.
4. Mathias B，Urs M，Helmut K，et al. The potential of the yeast Debaryomyces hansenii H525 to degrade biogenic amines in food[J]. Microorganisms，2015，3(4): 839-850.
5. Yoshinori S， Hiroko M， Akira Y， et al. A thermostable histamine oxidase from Arthrobacter crystallopoietes KAIT-B-007[J]. Journal of Bioscience and Bioengineering，2004，97(2): 104-110. 45.
6. Lee JI， Kim Y W. Characterization of amine oxidases from Arthrobacter aurescens and application for determination of biogenic amines[J]. World J Microbiol Biotechnol，2013，29(4): 673-682.

Sequence and Features

Assembly Compatibility:

• 10
  COMPATIBLE WITH RFC[10]
• 12
  COMPATIBLE WITH RFC[12]
• 21
  INCOMPATIBLE WITH RFC[21]

  Illegal BamHI site found at 2197
  
• 23
  COMPATIBLE WITH RFC[23]
• 25
  INCOMPATIBLE WITH RFC[25]

  Illegal NgoMIV site found at 15
  Illegal NgoMIV site found at 1104
  
• 1000
  INCOMPATIBLE WITH RFC[1000]

  Illegal BsaI.rc site found at 1188