scholarly journals Mutation of Arabidopsis Copper-Containing Amine Oxidase Gene AtCuAOδ Alters Polyamines, Reduces Gibberellin Content and Affects Development

2020 ◽  
Vol 21 (20) ◽  
pp. 7789
Author(s):  
Basmah Alharbi ◽  
Julie D. Hunt ◽  
Simone Dimitrova ◽  
Natasha D. Spadafora ◽  
Alex P. Cort ◽  
...  
Keyword(s):  
Seed Germination ◽  
Gene Family ◽  
Amine Oxidase ◽  
Amine Oxidases ◽  
Oxidase Gene ◽  
Shoot Height ◽  
Leaf Emergence ◽  
Gibberellin Content ◽  
Delayed Flowering ◽  
Mutant Lines

Polyamines (PAs) are essential metabolites in plants performing multiple functions during growth and development. Copper-containing amine oxidases (CuAOs) catalyse the catabolism of PAs and in Arabidopsis thaliana are encoded by a gene family. Two mutants of one gene family member, AtCuAOδ, showed delayed seed germination, leaf emergence, and flowering time. The height of the primary inflorescence shoot was reduced, and developmental leaf senescence was delayed. Siliques were significantly longer in mutant lines and contained more seeds. The phenotype of AtCuAOδ over-expressors was less affected. Before flowering, there was a significant increase in putrescine in AtCuAOδ mutant leaves compared to wild type (WT), while after flowering both spermidine and spermine concentrations were significantly higher than in WT leaves. The expression of GA (gibberellic acid) biosynthetic genes was repressed and the content of GA1, GA7, GA8, GA9, and GA20 was reduced in the mutants. The inhibitor of copper-containing amine oxidases, aminoguanidine hydrochloride, mimicked the effect of AtCuAOδ mutation on WT seed germination. Delayed germination, reduced shoot height, and delayed flowering in the mutants were rescued by GA3 treatment. These data strongly suggest AtCuAOδ is an important gene regulating PA homeostasis, and that a perturbation of PAs affects plant development through a reduction in GA biosynthesis.

scholarly journals Developmental, hormone- and stress-modulated expression profiles of four members of the Arabidopsis copper-amine oxidase gene family

2020 ◽  
Vol 147 ◽  
pp. 141-160 ◽  
Author(s):  
Ilaria Fraudentali ◽  
Sandip A. Ghuge ◽  
Andrea Carucci ◽  
Paraskevi Tavladoraki ◽  
Riccardo Angelini ◽  
...  
Keyword(s):  
Gene Family ◽  
Amine Oxidase ◽  
Expression Profiles ◽  
Copper Amine Oxidase ◽  
Oxidase Gene ◽  
Copper Amine

scholarly journals Unique protonation states of aspartate and topaquinone in the active site of copper amine oxidase

RSC Advances ◽  
2020 ◽  
Vol 10 (63) ◽  
pp. 38631-38639
Author(s):  
Mitsuo Shoji ◽  
Takeshi Murakawa ◽  
Mauro Boero ◽  
Yasuteru Shigeta ◽  
Hideyuki Hayashi ◽  
...  
Keyword(s):  
Biogenic Amines ◽  
Active Site ◽  
Amine Oxidase ◽  
First Principle ◽  
Amine Oxidases ◽  
Oxidative Deamination ◽  
Copper Amine Oxidase ◽  
First Principle Calculations ◽  
Copper Amine Oxidases ◽  
Copper Amine

Copper amine oxidases catalyze the oxidative deamination of biogenic amines. We investigated the unique protonation states in the active site using first-principle calculations.

Cloning and sequencing of the peroxisomal amine oxidase gene from Hansenula polymorpha

1989 ◽  
Vol 1008 (2) ◽  
pp. 157-167 ◽  
Author(s):  
Paul G Bruinenberg ◽  
Melchior Evers ◽  
Hans R Waterham ◽  
Jeroen Kuipers ◽  
Annika C Arnberg ◽  
...  
Keyword(s):  
Amine Oxidase ◽  
Hansenula Polymorpha ◽  
Cloning And Sequencing ◽  
Oxidase Gene

scholarly journals The amine oxidases of human placenta and pregnancy plasma

1974 ◽  
Vol 139 (1) ◽  
pp. 169-181 ◽  
Author(s):  
William G. Bardsley ◽  
M. James C. Crabbe ◽  
Ian V. Scott
Keyword(s):  
Diamine Oxidase ◽  
Amine Oxidase ◽  
Enzyme System ◽  
Placental Tissue ◽  
Amine Oxidases ◽  
Rate Limiting Step ◽  
Limiting Step ◽  
Ping Pong ◽  
Normal Human ◽  
Rate Limiting

1. The purification of monoamine oxidase and diamine oxidase from normal human term placental tissue is described. 2. The properties of these enzymes are reported and compared with the properties of unpurified human pregnancy plasma. 3. This comparison shows that the amine oxidase of pregnancy plasma has properties corresponding to purified placental diamine oxidase, suggesting a placental origin for the plasma enzyme system. 4. Detailed kinetic study of the purified placental diamine oxidase suggests that it has a Ping Pong sequence, a mechanism of action and rate-limiting step similar to the diamine oxidase of pig kidney. 5. It is suggested that the enzyme system is important in protecting the foeto-placental unit from excesses of biogenic amines.

scholarly journals An amine oxidase gene from mud crab, Scylla paramamosain, regulates the neurotransmitters serotonin and dopamine in vitro

PLoS ONE ◽  
2018 ◽  
Vol 13 (9) ◽  
pp. e0204325
Author(s):  
Junguo Liu ◽  
Ming Zhao ◽  
Wei Song ◽  
Lingbo Ma ◽  
Xiu Li ◽  
...  
Keyword(s):  
Amine Oxidase ◽  
Scylla Paramamosain ◽  
Mud Crab ◽  
Oxidase Gene

scholarly journals Cloning of a Novel Nicotine Oxidase Gene from Pseudomonas sp. Strain HZN6 Whose Product Nonenantioselectively Degrades Nicotine to Pseudooxynicotine

2013 ◽  
Vol 79 (7) ◽  
pp. 2164-2171 ◽  
Author(s):  
Jiguo Qiu ◽  
Yun Ma ◽  
Jing Zhang ◽  
Yuezhong Wen ◽  
Weiping Liu
Keyword(s):  
Amine Oxidase ◽  
Sole Source ◽  
Site Directed Mutagenesis ◽  
Broad Host Range ◽  
Upstream Sequence ◽  
Oxidase Gene ◽  
Content Type ◽  
Reading Frame ◽  
Degrading Bacteria ◽  
Nicotine Degradation

ABSTRACTPseudomonassp. strain HZN6 utilizes nicotine as its sole source of carbon, nitrogen, and energy. However, its catabolic mechanism has not been elucidated. In this study, self-formed adaptor PCR was performed to amplify the upstream sequence of the pseudooxynicotine amine oxidase gene. A 1,437-bp open reading frame (designatednox) was found to encode a nicotine oxidase (NOX) that shows 30% amino acid sequence identity with 6-hydroxy-l-nicotine oxidase fromArthrobacter nicotinovorans. Thenoxgene was cloned into a broad-host-range cloning vector and transferred into the non-nicotine-degrading bacteriaEscherichia coliDH5α (DH-nox) andPseudomonas putidaKT2440 (KT-nox). The transconjugant KT-nox obtained nicotine degradation ability and yielded an equimolar amount of pseudooxynicotine, while DH-nox did not. Reverse transcription-PCR showed that thenoxgene is expressed in both DH5α and KT2440, suggesting that additional factors required for nicotine degradation are present in aPseudomonasstrain(s), but not inE. coli. The mutant of strain HZN6 withnoxdisrupted lost the ability to degrade nicotine, but not pseudooxynicotine. These results suggested that thenoxgene is responsible for the first step of nicotine degradation. The (RS)-nicotine degradation results showed that the two enantiomers were degraded at approximately the same rate, indicating that NOX does not show chiral selectivity. Site-directed mutagenesis revealed that both the conserved flavin adenine dinucleotide (FAD)-binding GXGXXG motif and His456 are essential for nicotine degradation activity.

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