Isolation and properties of L-lysine-α-oxidase from the fungus Trichoderma cf. aureoviride RIFAI VKM F-4268D

Arinbasarova, A. Yu.; Ashin, V. V.; Makrushin, K. V.; Меденцев, А. Г.; Лукашева, Е. В.; Березов, Т. Т.

doi:10.1134/s0026261712050037

Cited by 12 publications

(17 citation statements)

References 18 publications

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“…As it was shown earlier [5] , LysOx is a homodimeric molecule with identical subunits (М.М. equal to 57–58 кDа), that assumes a cooperative substrate binding.…”

Section: Resultsmentioning

confidence: 79%

“…LysOx was isolated from the fungus Trichoderma cf. aureoviride Rifai VKM F-4268D as described earlier [5] . Homogenous enzyme preparation of high purity (310 fold) with high specific activity (equal to 90 U/mg of protein) was used in the present work.…”

Section: Methodsmentioning

confidence: 99%

“…aureoviride Rifai ВКМ F-4268D. The homogenous enzyme with high specific activity (equal to 90 E/mg of protein) was obtained [5] , and its significant anti-proliferative properties were demonstrated [4] . Considerable cytotoxicity and anti-tumor effects was shown in vitro against a panel of murine and human tumor cell lines and in vivo on murine tumors and on animals with human tumor xenografts (breast cancer SKBR3, melanoma Bro, colon cancer HCT116 and ovarian adenocarcinoma SCOV3) [4] .…”

Section: Introductionmentioning

confidence: 98%

“…Earlier, we have reported [5] about LysOx isolated from the extracellular growth medium of Trichoderma cf. aureoviride Rifai ВКМ F-4268D.…”

Section: Introductionmentioning

confidence: 99%

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Kinetic characteristics of L-lysine α- oxidase from Trichoderma cf. aureoviride Rifai VKM F-4268D: Substrate specificity and allosteric effects

Krupyanko

Меденцев

Лукашева

et al. 2017

Biochemistry and Biophysics Reports

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The present work aims to investigate the kinetic characteristics of homodimer enzyme L-lysine α-oxidase from Trichoderma cf. aureoviride Rifai VKM F-4268D, taking into account allosteric effects. The enzyme was first shown to reveal positive cooperativeness, h=2.05±0.15. Using additional opportunities of Hill coefficient the value of the Michaelis–Menten constant has been estimated, Km=1.015∙10−5М, indicating high strength of substrate binding to the active site of each subunit. High selectivity and absolute L-stereospecificity of the enzyme were shown. The inhibition of L-lysine conversion by non-cleavable lysine analogs as well as the reaction product was found out to take place. These effects have been evaluated only as the inhibition coefficients (%). A more detailed study of these inhibition effects was complicated because of the cooperativeness of enzyme subunits mentioned above. The kinetic scheme of L-lysine α-oxidase was proposed involving parallel-subsequent action of each of two subunits in the catalytic act.We think that the results obtained will be useful for studying the kinetic properties of other multi-subunit enzymes and improve understanding of the mechanisms of their action.

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“…As it was shown earlier [5] , LysOx is a homodimeric molecule with identical subunits (М.М. equal to 57–58 кDа), that assumes a cooperative substrate binding.…”

Section: Resultsmentioning

confidence: 79%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 98%

“…Earlier, we have reported [5] about LysOx isolated from the extracellular growth medium of Trichoderma cf. aureoviride Rifai ВКМ F-4268D.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Kinetic characteristics of L-lysine α- oxidase from Trichoderma cf. aureoviride Rifai VKM F-4268D: Substrate specificity and allosteric effects

Krupyanko

Меденцев

Лукашева

et al. 2017

Biochemistry and Biophysics Reports

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“…Amano et al and Arinbasarova et al have previously characterized the recombinant enzyme of RaiP from Trichoderma viride (Amano et al, 2015; Arinbasarova et al, 2012). However, the reported specific activities of the purified enzyme was just 80 or 90 U/mg in the previous studies, which are about 11% of the specific activity we measured in this study.…”

Section: Resultsmentioning

confidence: 99%

Production of nonnatural straight-chain amino acid 6-aminocaproate via an artificial iterative carbon-chain-extension cycle

Cheng

Song²,

Wang³

et al. 2019

Preprint

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22Bioplastics produced from microbial source are promising green alternatives to 23 traditional petrochemical-derived plastics. Nonnatural straight-chain amino acids, 24 especially 5-aminovalerate, 6-aminocaproate and 7-aminoheptanoate are potential 25 monomers for the synthesis of polymeric bioplastics as their primary amine and 26 carboxylic acid are ideal functional groups for polymerization. Previous pathways for 27 5-aminovalerate and 6-aminocaproate biosynthesis in microorganisms are derived from 28 L-lysine catabolism and citric acid cycle, respectively. Here, we show the construction 29 of an artificial iterative carbon-chain-extension cycle in Escherichia coli for 30 simultaneous production of a series of nonnatural amino acids with varying chain length. 31 Overexpression of L-lysine α-oxidase in E. coli yields 2-keto-6-aminocaproate as a 32 non-native substrate for the artificial iterative carbon-chain-extension cycle. The chain-33 extended α-ketoacid is subsequently decarboxylated and oxidized by an α-ketoacid 34 decarboxylase and an aldehyde dehydrogenase, respectively, to yield the nonnatural 35 straight-chain amino acid products. The engineered system demonstrated simultaneous 36 in vitro production of 99.16 mg/L of 5-aminovalerate, 46.96 mg/L of 6-aminocaproate 37 and 4.78 mg/L of 7-aminoheptanoate after 8 hours of enzyme catalysis starting from 2-38 keto-6-aminocaproate as the substrate. Furthermore, simultaneous production of 2.15 39 g/L of 5-aminovalerate, 24.12 mg/L of 6-aminocaproate and 4.74 mg/L of 7-40 aminoheptanoate was achieved in engineered E. coli. This work illustrates a promising 41 metabolic-engineering strategy to access other medium-chain organic acids with -NH2, 42 -SCH3, -SOCH3, -SH, -COOH, -COH, or -OH functional groups through carbon-chain-43 elongation chemistry.44 Keywords: Nonnatural straight chain amino acid, 6-Aminocaproate, Carbon chain 45 elongation, Synthetic biology, Iterative cycle 46 3 47 Abbreviations: 48 NNSCAA, Nonnatural straight chain amino acid; 5AVA, 5-Aminovalerate; 6ACA, 6-49

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Plasma pharmacokinetics and tissue distribution of L-lysine α-oxidase from Trichoderma cf. aureoviride RIFAI VKM F- 4268D in mice

et al. 2021

View full text Add to dashboard Cite

Isolation and properties of L-lysine-α-oxidase from the fungus Trichoderma cf. aureoviride RIFAI VKM F-4268D

Cited by 12 publications

References 18 publications

Kinetic characteristics of L-lysine α- oxidase from Trichoderma cf. aureoviride Rifai VKM F-4268D: Substrate specificity and allosteric effects

Kinetic characteristics of L-lysine α- oxidase from Trichoderma cf. aureoviride Rifai VKM F-4268D: Substrate specificity and allosteric effects

Production of nonnatural straight-chain amino acid 6-aminocaproate via an artificial iterative carbon-chain-extension cycle

Plasma pharmacokinetics and tissue distribution of L-lysine α-oxidase from Trichoderma cf. aureoviride RIFAI VKM F- 4268D in mice

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