scholarly journals Microbial oxidation of amines. Distribution, purification and properties of two primary-amine oxidases from the yeast Candida boidinii grown on amines as sole nitrogen source

1981 ◽  
Vol 199 (1) ◽  
pp. 187-201 ◽  
Author(s):  
Geoffrey W. Haywood ◽  
Peter J. Large
Keyword(s):  
Amino Acids ◽  
Amine Oxidase ◽  
Primary Amines ◽  
Carbon Chain Length ◽  
Candida Boidinii ◽  
Amine Oxidases ◽  
Microbial Oxidation ◽  
Ph Optimum ◽  
Benzylamine Oxidase ◽  
As If

1. The yeast Candida boidinii was grown on glucose as carbon source with a range of amines and amino acids as nitrogen sources. Cells grown on amines contained elevated activities of catalase. If the amines contained N-methyl groups, formaldehyde dehydrogenase, formate dehydrogenase and S-formylglutathione hydrolase were also elevated in activity compared with cells grown on (NH4)2SO4. 2. Cells grown on all the amines tested, but not those grown on urea or amino acids, contained an oxidase attacking primary amines, which is referred to as methylamine oxidase. In addition, cells grown on some amines contained a second amine oxidase, which is referred to as benzylamine oxidase. 3. Both amine oxidases were purified to near homogeneity. 4. Benzylamine oxidase was considerably more stable at 45 and 50°C than was methylamine oxidase. 5. Both enzymes had a pH optimum in the region of 7.0, and had a considerable number of substrates in common. There were, however, significant differences in the substrate specificity of the two enzymes. The ratio V/Kapp.m increased with increasing n-alkyl carbon chain length for benzylamine oxidase, but decreased for methylamine oxidase. 6. Both enzymes showed similar sensitivity to carbonyl-group reagents, copper-chelating agents and other typical ‘diamine oxidase inhibitors’. 7. The stoicheiometry for the reaction catalysed by each enzyme was established. 8. The kinetics of methylamine oxidase were examined by varying the methylamine and oxygen concentrations in turn. A non-Ping Pong kinetic pattern with intersecting double-reciprocal plots was obtained, giving Km values of 10mum for O2 and 198mum for methylamine. The significance of this unusual kinetic behaviour is discussed. Similar experiments were not possible with the benzylamine oxidase, because it seemed to have an even lower Km for O2. 9. Both enzymes had similar subunit Mr values of about 80000, but the benzylamine oxidase behaved as if it were usually a dimer, Mr 136000, which under certain conditions aggregated to a tetramer, Mr 288000. Methylamine oxidase was mainly in the form of an octamer, Mr 510000, which gave rise quite readily to dimers of Mr 150000, and on gel filtration behaved as if the Mr was 286000.

scholarly journals Microbial oxidation of amines. Partial purification of a mixed-function secondary-amine oxidase system from Pseudomonas aminovorans that contains an enzymically active cytochrome-P-420-type haemoprotein

1971 ◽  
Vol 125 (2) ◽  
pp. 449-459 ◽  
Author(s):  
R. R. Eady ◽  
T. R. Jarman ◽  
P. J. Large
Keyword(s):  
Carbon Monoxide ◽  
Amine Oxidase ◽  
Enzyme System ◽  
Reaction Rates ◽  
Secondary Amines ◽  
Partial Purification ◽  
Microbial Oxidation ◽  
Ph Optimum ◽  
Spectral Maximum ◽  
Extractable Iron

1. Crude extracts of Pseudomonas aminovorans grown on methylamine, di-methylamine, trimethylamine or trimethylamine N-oxide contain an enzyme or enzyme system catalysing the NADH- or NADPH- and oxygen-dependent oxidation of dimethylamine to methylamine and formaldehyde. 2. The enzyme has been partially purified about five-fold. It is unstable, but can be stabilized by addition of 5% (v/v) ethanol. 3. The partially purified enzyme will utilize either NADH (Km 6.5μm) or NADPH (Km 13.2μm): The following secondary amines have been shown to be substrates: dimethylamine, ethylmethylamine, diethylamine, methyl-n-propylamine, ethyl-n-propylamine, n-butylmethylamine and N-methylethanolamine. The Km values and comparative reaction rates for each substrate have been determined. Where the alkyl groups are different, the aldehyde products are derived from both groups. 4. The enzyme system has a pH optimum of 6.8 and is inhibited by mercurials, thiol compounds, cyanide and carbon monoxide. 5. The partially purified preparation had a spectral maximum at 412nm with shoulders at 427 and 550nm. Reduction with dithionite or NAD(P)H bleached the 412nm peak, and the shoulder at 427nm became a peak. Additional peaks appeared at 550 and 580–588nm. Reduction of a preparation bubbled with carbon monoxide enhanced and sharpened the Soret peak and caused it to shift to 422nm. 6. Analysis of the preparation showed the presence of flavin, acid-extractable iron and non-acid-extractable iron in the proportion 1.1:1.9:1. On reduction with dithionite or NADPH the preparation showed an electron-paramagnetic-resonance signal at around g=1.946.

Spermine oxidase and benzylamine oxidase. Distribution, development and substrate specificity

1962 ◽  
Vol 156 (963) ◽  
pp. 268-279 ◽  
Keyword(s):  
Blood Plasma ◽  
Amine Oxidase ◽  
Enzymic Activity ◽  
Secondary Amines ◽  
Spermine Oxidase ◽  
Amine Oxidases ◽  
Newborn Piglets ◽  
Wood Shavings ◽  
Mammalian Blood ◽  
Benzylamine Oxidase

A survey has been made of the distribution of the two types of amine oxidase that occur in mammalian blood plasma. Spermine oxidase has been found in all ruminants (Ruminantia and Tylopoda) examined, and also in the hippopotamus and two members of the order Hyracoidea. Benzylamine oxidase has a much wider distribution; it occurs not only in Ungulates and Carnivores, but has also been found in some Primates. Benzylamine oxidase was not found in the blood plasma of newborn piglets; in newborn foals the enzymic activity was low. Spermine oxidase activity, absent or very low in the newborn kid, developed at similar rates in kids kept with the mother, bedded on straw, and in those removed from the mother and bedded on wood shavings. The plasma amine oxidases differ from the intracellular amine oxidase in that they are unable to oxidize N -methylated secondary amines.

Three types of stereospecificity and the kinetic deuterium isotope effect in the oxidative deamination of dopamine as catalyzed by different amine oxidases

1988 ◽  
Vol 66 (8) ◽  
pp. 853-861 ◽  
Author(s):  
Peter H. Yu
Keyword(s):  
Isotope Effect ◽  
Amine Oxidase ◽  
Deuterium Atom ◽  
Amine Oxidases ◽  
Deuterium Isotope Effect ◽  
Plasma Amine Oxidase ◽  
Benzylamine Oxidase ◽  
Rate Limiting ◽  
Hog Kidney ◽  
Pea Seedling

When the stereospecifically deuterated dopamine enantiomers, (R)- and (S)-[α-2H1]dopamine, are incubated with amine oxidases, the deuterium atom may be either retained to form monodeuterated 3,4-dihydroxyphenylacetaldehyde, or eliminated to produce the nondeuterated or protio-aldehyde product. These two aldehydes can be separated from one another and identified by high-performance liquid chromatography with electrochemical detection. Three types of stereospecific abstraction of a hydrogen from the α-carbon of dopamine during deamination have been observed. In the first type, the pro-R hydrogen is removed from the α-carbon. Enzymes in this category are mitochondrial monoamine oxidases A and B, as isolated from different tissues and species. The second type of deamination involves the abstraction of pro-S hydrogen from the α-carbon of dopamine. Soluble enzymes, such as rat aorta benzylamine oxidase or diamine oxidase from hog kidney and pea seedling, have been found to belong to this group. Bovine plasma amine oxidase exhibits the third type of deamination where no absolute stereospecificity is required. This enzyme catalyzes the oxidation of either (S)- or (R)-[α-2H1]dopamine, preferably breaking the C—H bond rather than the C—2H bond in both cases. The kinetic deuterium isotope effect during the deamination of dopamine catalyzed by the different amine oxidases varies greatly; VH/VD ranges from 1.5 to 5.5. The high magnitude of the isotope effect suggests that hydrogen abstraction may be the rate-limiting step (i.e., in reactions catalyzed by benzylamine oxidase and monoamine oxidase). When the isotope effect is low (i.e., for diamine oxidases from hog kidney or pea seedling), it is uncertain if the breaking of the bond is rate limiting.

Tandem Alkylation/Michael Addition Reaction of Dithiocarbamic Acids with Alkyl γ-Bromocrotonates: Access to Functionalized 1,3-Thiazolidine-2-thiones

Synthesis ◽  
2021 ◽  
Author(s):  
Azim Ziyaei Halimehjani ◽  
Petr Beier ◽  
Maryam Khalili Foumeshi ◽  
Ali Alaei ◽  
Blanka Klepetářová
Keyword(s):  
Amino Acids ◽  
Carbon Disulfide ◽  
Multicomponent Reaction ◽  
Michael Addition ◽  
Addition Reaction ◽  
Primary Amines ◽  
Oxidation Reactions ◽  
Michael Addition Reaction ◽  
Synthetic Utility ◽  
Reaction Proceeds

AbstractThiazolidine-2-thiones were prepared via a novel multicomponent reaction of primary amines (amino acids), carbon disulfide, and γ-bromocrotonates. The reaction proceeds via a domino alkylation/intramolecular Michael addition to provide the corresponding thiazolidine-2-thiones in high to excellent yields. By using diamines in this protocol, bis(thiazolidine-2-thiones) derivatives were synthesized. The synthetic utility of the adducts was demonstrated by hydrolysis, amidation, and oxidation reactions.

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.

Titration syntheses of polyaminosubstituted phthalocyanines via nucleophilic aromatic substitutions on zinc(II) 1,2,3,4,8,9,10,11,15,16,17,18,22,23,24,25-hexadecafluorophthalocyanine

2007 ◽  
Vol 11 (07) ◽  
pp. 537-546 ◽  
Author(s):  
Clifford C. Leznoff ◽  
Annette Hiebert ◽  
Sibel Ok
Keyword(s):  
Amino Acids ◽  
Chain Length ◽  
Secondary Amines ◽  
Primary Amines ◽  
Tertiary Butyl ◽  
Butyl Esters ◽  
Mild Conditions ◽  
Nucleophilic Aromatic Substitutions

Primary amines, secondary amines and tertiary butyl esters of amino acids are used as nucleophiles with zinc(II) hexadecafluorophthalocyanine to provide mixtures of mono and disubstituted fluorinated phthalocyanines under mild conditions, or polyaminosubstituted phthalocyanines when using the amines as solvents. Diamines give cyclic substituted phthalocyanines, binuclear or trinuclear phthalocyanines or mixtures of both types, depending on the chain length or structure of the diamine.

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.

Reaction of N-acylated ?-amino acids with primary amines

1978 ◽  
Vol 27 (5) ◽  
pp. 963-969
Author(s):  
G. Ya. Kondrat'eva ◽  
M. A. Aitzhanova ◽  
V. S. Bogdanov ◽  
Z. N. Ivanova
Keyword(s):  
Amino Acids ◽  
Primary Amines
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