Assembly of amine oxidase andD-amino acid oxidase in the cytosol of peroxisome-deficient mutants of theyeast Hansenula polymorpha during growth of cells on glucose in the presence of primary amines orD-alanine as the sole nitrogen source

Yeast ◽  
1990 ◽  
Vol 6 (6) ◽  
pp. 501-509 ◽  
Author(s):  
G. J. Sulter ◽  
I. J. Van Der Klei ◽  
W. Harder ◽  
M. Veenhuis
Keyword(s):  
Amino Acid ◽  
Nitrogen Source ◽  
Amine Oxidase ◽  
Hansenula Polymorpha ◽  
Primary Amines ◽  
Acid Oxidase ◽  
Sole Nitrogen Source ◽  
Amino Acid Oxidase

Enzymic Oxidation of Amines in Decapods

1954 ◽  
Vol 31 (1) ◽  
pp. 1-7
Author(s):  
H. BLASCHKO ◽  
JEAN M. HIMMS
Keyword(s):  
Amino Acid ◽  
Amine Oxidase ◽  
Acid Oxidase ◽  
Sepia Officinalis ◽  
Amino Acid Oxidase ◽  
Enzymic Oxidation ◽  
Related Compounds ◽  
Long Chain

1. The enzyme amine oxidase has been found in many organs of Sepia officinalis and of Loligo forbesii. 2. The enzyme oxidizes not only tyramine and related compounds, e.g. p-hydroxyphenylethanolamine (‘octopamine’) and β-phenylethylamine, but also aliphatic monoarnines and long-chain diamines as well as tryptamine and 5-hydroxytryptamlne. 3. The liver of Loligo contains D-amino-acid oxidase.

scholarly journals Amino Acid Catabolism by an areA-Regulated Gene Encoding an l-Amino Acid Oxidase with Broad Substrate Specificity in Aspergillus nidulans

2005 ◽  
Vol 71 (7) ◽  
pp. 3551-3555 ◽  
Author(s):  
Meryl A. Davis ◽  
Marion C. Askin ◽  
Michael J. Hynes
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Substrate Specificity ◽  
Nitrogen Source ◽  
Aspergillus Nidulans ◽  
Nitrogen Sources ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Broad Substrate Specificity ◽  
Strong Growth

ABSTRACT The filamentous fungus Aspergillus nidulans can use a wide range of compounds as nitrogen sources. The synthesis of the various catabolic enzymes needed to breakdown these nitrogen sources is regulated by the areA gene, which encodes a GATA transcription factor required to activate gene expression under nitrogen-limiting conditions. The areA102 mutation results in pleiotropic effects on nitrogen source utilization, including better growth on certain amino acids as nitrogen sources. Mutations in the sarA gene were previously isolated as suppressors of the strong growth of an areA102 strain on l-histidine as a sole nitrogen source. We cloned the sarA gene by complementation of a sarA mutant and showed that it encodes an l-amino acid oxidase enzyme with broad substrate specificity. Elevated expression of this enzyme activity in an areA102 background accounts for the strong growth of these strains on amino acids that are substrates for this enzyme. Loss of function sarA mutations, which abolish the l-amino acid oxidase activity, reverse the areA102 phenotype. Growth tests with areA102 and sarA mutants show that this enzyme is the primary route of catabolism for some amino acids, while other amino acids are metabolized through alternative pathways that yield either ammonium or glutamate for growth.

Investigations about various Possible Functions of the L -Amino Acid Oxidase in the Cyanobacterium Anacystis nidulans

1989 ◽  
Vol 44 (5-6) ◽  
pp. 370-377 ◽  
Author(s):  
Elfriede K. Pistorius ◽  
Regine Kertsch ◽  
Susanne Faby
Keyword(s):  
Amino Acid ◽  
Photosystem Ii ◽  
Divalent Cation ◽  
Anacystis Nidulans ◽  
Acid Oxidase ◽  
Sole Nitrogen Source ◽  
Amino Acid Oxidase ◽  
Cation Concentration ◽  
Arginine Catabolism ◽  
Photosystem Ii Activity

Abstract The cyanobacterium A nacystis nidulans was grown on nitrate or L-arginine as sole nitrogen source and in the presence of different divalent cation concentrations (1 mᴍ MgSO4 and 0.1 mᴍ CaCl2 or 0.1 mᴍ MgSO4 and 0.05 mᴍ CaCl2). The L-amino acid oxidase previously reported to be present in Anacystis nidulans (E . K. Pistorius and A. E. Gau, Biochim. Biophys. Acta 849, 203, 1986) was shown to be involved in L-arginine catabolism in cells grown with the lower divalentcation concentration. Under these conditions L-arginine was partly degraded via 2-ketoarginine and 4-guanidinobutyrate. On the other hand, at higher cation concentrations the ʟ-amino acid oxidase activity seem ed to be not sufficient to provide enough NH4+ from ʟ-arginine for cell growth. Under those conditions photosystem II activity was initially reduced, and growth on ʟ-arginine could only start after photosystem II activity increased again and after arginase was induced. The arginase pathway was functional in A . nidulans grown on ʟ-arginine independently of the divalent cation concentration in the medium. A tentative scheme of the various functiona roles of the ʟ-amino acid oxidase protein in A . nidulans is given. This model combines the here presented and the previous results and suggests that the ʟ-amino acid oxidase is functional in photosynthetic and respiratory activities as well as in ʟ-arginine degradation in A . nidulans. All these activities of the ʟ-amino acid oxidase protein are greatly influenced by the divalent cation concentration in the growth medium.

scholarly journals Mechanistic Studies of an Amine Oxidase Derived from d-Amino Acid Oxidase

Biochemistry ◽  
2017 ◽  
Vol 56 (14) ◽  
pp. 2024-2030 ◽  
Author(s):  
Elizabeth E. Trimmer ◽  
Udayanga S. Wanninayake ◽  
Paul F. Fitzpatrick
Keyword(s):  
Amino Acid ◽  
Amine Oxidase ◽  
Acid Oxidase ◽  
Mechanistic Studies ◽  
Amino Acid Oxidase

scholarly journals Mechanisms of copper loading on the Schizosaccharomyces pombe copper amine oxidase 1 expressed in Saccharomyces cerevisiae

Microbiology ◽  
2006 ◽  
Vol 152 (9) ◽  
pp. 2819-2830 ◽  
Author(s):  
Julie Laliberté ◽  
Simon Labbé
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Schizosaccharomyces Pombe ◽  
Nitrogen Source ◽  
Oxidase Activity ◽  
Amine Oxidase ◽  
Yeast Cells ◽  
Primary Amines ◽  
Sole Nitrogen Source ◽  
Amine Oxidase Activity ◽  
Copper Amine

Copper amine oxidases (CAOs) are found in almost every living kingdom. Although Saccharomyces cerevisiae is one of the few yeast species that lacks an endogenous CAO, heterologous gene expression of CAOs from other organisms produces a functional enzyme. To begin to characterize their function and mechanisms of copper acquisition, two putative cao + genes from Schizosaccharomyces pombe were expressed in S. cerevisiae. Expression of spao1 + resulted in the production of an active enzyme capable of catalysing the oxidative deamination of primary amines. On the other hand, expression of spao2 + failed to produce an active CAO. Using a functional spao1 +–GFP fusion allele, the SPAO1 protein was localized in the cytosol. Under copper-limiting conditions, yeast cells harbouring deletions of the MAC1, CTR1 and CTR3 genes were defective in amine oxidase activity. Likewise, atx1Δ null cells exhibited no CAO activity, while ccc2Δ mutant cells exhibited decreased levels of amine oxidase activity, and mutations in cox17Δ and ccs1Δ did not cause any defects in this activity. Copper-deprived S. cerevisiae cells expressing spao1 + required a functional atx1 + gene for growth on minimal medium containing ethylamine as the sole nitrogen source. Under these conditions, the inability of the atx1Δ cells to utilize ethylamine correlated with the lack of SPAO1 activity, in spite of the efficient expression of the protein. Cells carrying a disrupted ccc2Δ allele exhibited only weak growth on ethylamine medium containing a copper chelator. The results of these studies reveal that expression of the heterologous spao1 + gene in S. cerevisiae is required for its growth in medium containing ethylamine as the sole nitrogen source, and that expression of an active Schiz. pombe SPAO1 protein in S. cerevisiae depends on the acquisition of copper through the high-affinity copper transporters Ctr1 and Ctr3, and the copper chaperone Atx1.

Purification and Characterization of Lupus Anticoagulant Like Protein from Agkistrodon Halys Brevicaudus Venom

1996 ◽  
Vol 76 (06) ◽  
pp. 0993-0997
Author(s):  
Zhao-Yan Li ◽  
Xiao-Wei Wu ◽  
Tie-Fu Yu ◽  
Eric C-Y Lian
Keyword(s):  
Amino Acid ◽  
Lupus Anticoagulant ◽  
Inhibitory Effect ◽  
Clotting Factor ◽  
Acid Oxidase ◽  
Crude Venom ◽  
Amino Acid Oxidase ◽  
Sds Page ◽  
The Individual ◽  
Reducing Condition

SummaryBy means of CM-Sephadex C-25, DEAE-Sephadex A-50, Sephadex G-200, and Sephadex G-75 chromatographies, a lupus anticoagulant like protein (LALP) from Agkistrodon halys brevicaudus was purified. On SDS-PAGE, the purified LALP had a molecular weight of 25,500 daltons under non-reducing condition and 15,000 daltons under reducing condition. The isoelectric point was pH 5.6. Its N terminal amino acid sequencing revealed a mixture of 2 sequences: DCP(P/S)(D/G)WSSYEGH(C/R)Q(Q/K). It was devoid of phospho-lipaseA, fibrino(geno)lytic, 5′-nucleotidase, L-amino acid oxidase, phosphomonoesterase, phosphodiesterase and thrombin-like activities, which were found in crude venom. In the presence of LALP, PT, aPTT, and dRVVT of human plasma were markedly prolonged and its effects were concentration-dependent but time-independent. The inhibitory effect of LALP on the plasma clotting time was enhanced by decreasing phospholipid concentration in TTI test. The individual clotting factor activity was not affected by LALP when higher dilutions of LALP-plasma mixture were used for assay. Russell’s viper venom time was shortened when high phospholipid confirmatory reagent was used. Therefore, the protein has lupus anticoagulant property.

Impairment of Platelet Aggregation by Echis colorata Venom Mediated by L-Amino Acid Oxidase or H2O2

1982 ◽  
Vol 48 (03) ◽  
pp. 277-282 ◽  
Author(s):  
I Nathan ◽  
A Dvilansky ◽  
T Yirmiyahu ◽  
M Aharon ◽  
A Livne
Keyword(s):  
Hydrogen Peroxide ◽  
Amino Acid ◽  
Platelet Aggregation ◽  
Snake Venom ◽  
Oxidase Activity ◽  
Enzyme Preparation ◽  
Acid Oxidase ◽  
Crude Venom ◽  
Amino Acid Oxidase ◽  
Hemostatic Disorders

SummaryEchis colorata bites cause impairment of platelet aggregation and hemostatic disorders. The mechanism by which the snake venom inhibits platelet aggregation was studied. Upon fractionation, aggregation impairment activity and L-amino acid oxidase activity were similarly separated from the crude venom, unlike other venom enzymes. Preparations of L-amino acid oxidase from E.colorata and from Crotalus adamanteus replaced effectively the crude E.colorata venom in impairment of platelet aggregation. Furthermore, different treatments known to inhibit L-amino acid oxidase reduced in parallel the oxidase activity and the impairment potency of both the venom and the enzyme preparation. H2O2 mimicked characteristically the impairment effects of L-amino acid oxidase and the venom. Catalase completely abolished the impairment effects of the enzyme and the venom. It is concluded that hydrogen peroxide formed by the venom L-amino acid oxidase plays a role in affecting platelet aggregation and thus could contribute to the extended bleeding typical to persons bitten by E.colorata.

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