Stereospecificity of enzymatic transamination of γ-aminobutyrate

Burnett, Gial; Walsh, Christopher E.; Yonaha, Kazuo; Toyama, Seizen; Soda, Kenji

doi:10.1039/c39790000826

Cited by 28 publications

(19 citation statements)

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“…Keller (50) has found IX-CF 3 alanine inactivates a pseudomonallX dialkylaminoacid transaminase and Alston et al (5 1) behavior of gabaculine as a suicide substrate with GABA-T (19) and 0) aminotransferases (20) where transamination of this cyclohexadienoid analog of GABA is followed by isomerization of the exocyclic imine to yield the rearomatized, nonhydrolyzable m-anthranilyl-PLP derivative in the active site. Soper & Manning (56) have found gabaculine to be a more promiscuous inactivator than originally throught since it knocks out Bacillus sphaericus D-amino acid transaminase (K) = 0.…”

Section: Inactivators Of Pyridoxal-p Enzymesmentioning

confidence: 97%

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Suicide Substrates, Mechanism-Based Enzyme Inactivators: Recent Developments

Ct¹

1984

Annu. Rev. Biochem.

299

121

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Section: Inactivators Of Pyridoxal-p Enzymesmentioning

confidence: 97%

“…a stoichiometric titration). Such c(!,ses are known or approached by gabaculine with GABA transaminase (18)(19)(20) and isatoic anhydride with chymotrypsin (21). They represent the limit in specificity and killing efficiency by this partition ratio criterion.…”

Section: Perspectives and Summarymentioning

confidence: 99%

Suicide Substrates, Mechanism-Based Enzyme Inactivators: Recent Developments

Ct¹

1984

Annu. Rev. Biochem.

299

121

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“…F-126 (176,000 Da (tetramer)). 24) TPF reacted with various ketone compounds, including keto acids, aromatic, aliphatic, and cyclic ketones, and aldehydes. Among the ketones tested, pyruvic acid was the best amino acceptor.…”

Section: Discussionmentioning

confidence: 99%

Purification and Characterization of a Novel (S)-Enantioselective Transaminase fromPseudomonas fluorescensKNK08-18 for the Synthesis of Optically Active Amines

Ito

Kawano

Hasegawa

et al. 2011

Bioscience, Biotechnology, and Biochemistry

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Pseudomonas fluorescens KNK08-18, showing (S)-selective transaminase activity, was isolated from soil by an enrichment culture method using (S)-7-methoxy-2-aminotetraline as the main nitrogen source. A transaminase was purified from the strain to homogeneity in seven steps. The relative mass of the enzyme was estimated to be 53 kDa on SDS-polyacrylamide gel electrophoresis and 120 kDa by gel filtration, suggesting a homodimeric structure. The optimal pH and temperature for enzyme activity were about 8.0-8.5 and 40 °C. The purified enzyme produced (S)-7-methoxy-2-aminotetraline, (S)-SMA, from 7-methoxy-2-tetralone (SMT) with high enantioselectivity. Although (S)-1-phenylethylamine was the best amino donor, β-alanine and 4-aminobutyric acid, which are good substrates for typical ω-amino acid transaminase (EC 2.6.1.18) and GABA transaminase (2.6.1.19), were not reacted. It aminated a broad range of carbonyl compounds containing aromatic, non-aromatic, and acidic and non-acidic substrates.

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“…Thus, we have demonstrated the removal of the p r o 4 hydrogen at the prochiral C2 carbon atom of 2-aminoethylphosphonic acid in F! aeruginosa as most of the examples cited in the literature, such as: bacterial [6] and mammalian [7] yaminobutyrate aminotransferases, bacterial L-lysine &-aminotransferase [8], bacterial [7] and mammalian [9] L-ornithine S-aminotransferase, remove exclusively the p r o 4 hydrogen from the prochiral m-carbon atom of amino donors. However, the labilization of the pro-R hydrogen was exceptionally found for the m-amino acid: pyruvate aminotransferase of Pseudomonas sp.…”

Section: Discussionmentioning

confidence: 99%

“…However, the labilization of the pro-R hydrogen was exceptionally found for the m-amino acid: pyruvate aminotransferase of Pseudomonas sp. F-126, which abstracts the pro-R hydrogen from the C4 carbon atom of y-aminobutyrate [6]. A particular case is also that of alanine aminotransferase which operates on glycine [lo].…”

Section: Discussionmentioning

confidence: 99%

Stereochemistry of the reaction catalysed by 2‐aminoethylphosphonate aminotransferase

Lacoste

Dumora

Balas

et al. 1993

European Journal of Biochemistry

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(R)-and (S)-2-amino[2-D,]ethylphosphonic acids ([2-D1]AEP) were synthesised to investigate the stereochemistry of the reaction catalysed by 2-aminoethylphosphonate aminotransferase from Pseudomonas aeruginosa. This enzyme catalyses the transfer of the amino group of AEP to pyruvate to produce 2-phosphonoacetaldehyde and alanine. The enzymic reaction proceeding through the abstraction of a proton from the Schiff-base complex formed between the enzyme-bound pyridoxal 5'-phosphate, and the substrate, was carried out in an aqueous buffer at pH 8.5; it was followed by high-field 'H-NMR measurements (SOOMHz, H,O) on an AMX 500 Bruker spectrometer. The spectra, recorded with chiral (R)-or (S)-[2-D1]AEP, both showed the methylenic signal (3.0 ppm), whereas (S)-[2-D1]AEP gave the additional aldehydic signal (CHO, 9.6 ppm). These data clearly show that AEP-aminotransferase catalyses the abstraction of the pro-S hydrogen atom at the prochiral C2 carbon of AEP. Furthermore, careful timing of NMR measurements over a 2-hour period allows us to show the occurrence of an isotopic effect.2-Aminoethylphosphonic acid (AEP) is a naturally occurring compound discovered in Protozoa collected from sheep mmen, then found in a variety of microorganisms and marine animals [l]. The ability to cleave the C-P bond of AEP is widespread among microorganisms, but not among plants and animals. The catabolism of AEP by Pseudomonas aeruginosa involves a double-step pathway, allowing this molecule to be a source of nitrogen, carbon and phosphorus for this bacterium [2]. The first step of this pathway implies an inducible specific 2-aminoethylphosphonate aminotransferase, requiring pyridoxal 5'-phosphate (pyridoxal-P), which we have purified and characterized [3]. This enzyme catalyses the transfer of the amino group of AEP to pyruvate to produce 2-phosphonoacetaldehyde and alanine according to Scheme 1.The aminotransferase-catalysed reaction proceeds through the abstraction of a proton from the Schiff-base complex formed between the enzyme-bound pyridoxal-P and the substrate [4]. Thus, w-aminotransferases, unlike a-aminotransferases, exhibit two stereochemical possibilities for the proton abstraction.

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Stereospecificity of enzymatic transamination of γ-aminobutyrate

Abstract: The stereospecific removal of the 4-fWo-8hydrogen of y-aminobutyrate (GABA) has been demonstrated with a bacterial w-amino acid : pyruvate aminotransferase, while stereospecific removal of the 4-pro-Shydrogen has been demonstrated with a-oxoglutarate requiring bacterial GA4BA transsminase.

Cited by 28 publications

References 0 publications

Suicide Substrates, Mechanism-Based Enzyme Inactivators: Recent Developments

Suicide Substrates, Mechanism-Based Enzyme Inactivators: Recent Developments

Purification and Characterization of a Novel (S)-Enantioselective Transaminase fromPseudomonas fluorescensKNK08-18 for the Synthesis of Optically Active Amines

Stereochemistry of the reaction catalysed by 2‐aminoethylphosphonate aminotransferase

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