Identification and development of amino acid oxidases

Asano, Yasuhisa; Yasukawa, Kazuyuki

doi:10.1016/j.cbpa.2018.10.020

Cited by 23 publications

(8 citation statements)

References 49 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Оксидази L-амінокислот (ЛАКО) були вперше ідентифіковані в отруті змій у 40-х роках ХХ-го сторіччя. С того часу властивості ЛАКО, одержаних із різних організмів, інтенсивно вивчаються, інтерес до досліджень ЛАКО дедалі зростає, оскільки ці токсичні ферменти мають лікувальні властивості та біотехнологічний потенціал [1][2][3][4][5].…”

Section: загальна характеристика оксидаз L-амінокислотunclassified

Оксидази L-Амінокислот: Одержання, Властивості Та Перспективи Використання

Гайда¹

2021

interconf

View full text Add to dashboard Cite

Проаналізовано наукову літературу за проблемою оксидаз L-амінокислот стосовно джерел їхнього накопичення, методів одержання, моніторингу каталітичної активності, характеристик ферментів та перспектив їхнього використання. Розроблено скринінгові кольорові експрес-тести виявлення L-аргініноксидази (ArgО), запропоновано схему очищення ArgО з шапинкового гриба Amanita phalloides. Препарати АргО виділено в аналітичних кількостях, вивчено деякі властивості ферменту, а саме, умови зберігання та субстратну специфічність.

show abstract

Section: загальна характеристика оксидаз L-амінокислотunclassified

Оксидази L-Амінокислот: Одержання, Властивості Та Перспективи Використання

Гайда¹

2021

interconf

View full text Add to dashboard Cite

show abstract

“…Despite the numerous KR applications proposed for LAAOs, their recombinant production in heterologous hosts has proven difficult (Pollegioni et al, 2013). Recent studies have greatly increased the knowledge on these enzymes (e.g., L-Trp-, L-Lys-, Gly-or L-Arg oxidases) which might boost the applications of LAAOs in the production of D-AA derivatives (Francis et al, 2017;Asano and Yasukawa, 2019). An L-Trp oxidase from L. aerocolonigenes has been successfully applied using two alternative chemoenzymatic MECs for the synthesis of different halogenated D-Trp derivatives ( Figure 4E; Schnepel et al, 2019).…”

Section: Amino Acid Oxidase-based Mecsmentioning

confidence: 99%

“…Amino acid oxidases (AAOs) are important biotechnological flavoenzymes catalyzing the oxygen-dependent oxidative deamination of D - or L -α-AAs, resulting in α-keto acids, ammonia and hydrogen peroxide (through an imino acid intermediate which can decompose spontaneously to the corresponding α-keto acid and NH 3 , Figure 4A ; Pollegioni et al, 2008 , 2013 ; Asano and Yasukawa, 2019 ). These enzymes have a wide variety of biomedical and biotechnological applications, including the production of different α-keto acids, important intermediate building blocks.…”

Section: Multienzymatic Cascades For the Production Of Ncaasmentioning

confidence: 99%

Overview on Multienzymatic Cascades for the Production of Non-canonical α-Amino Acids

Martínez‐Rodríguez

Torres

Sánchez

et al. 2020

Front. Bioeng. Biotechnol.

View full text Add to dashboard Cite

The 22 genetically encoded amino acids (AAs) present in proteins (the 20 standard AAs together with selenocysteine and pyrrolysine), are commonly referred as proteinogenic AAs in the literature due to their appearance in ribosome-synthetized polypeptides. Beyond the borders of this key set of compounds, the rest of AAs are generally named imprecisely as non-proteinogenic AAs, even when they can also appear in polypeptide chains as a result of post-transductional machinery. Besides their importance as metabolites in life, many of D-α-and L-α-"non-canonical" amino acids (NcAAs) are of interest in the biotechnological and biomedical fields. They have found numerous applications in the discovery of new medicines and antibiotics, drug synthesis, cosmetic, and nutritional compounds, or in the improvement of protein and peptide pharmaceuticals. In addition to the numerous studies dealing with the asymmetric synthesis of NcAAs, many different enzymatic pathways have been reported in the literature allowing for the biosynthesis of NcAAs. Due to the huge heterogeneity of this group of molecules, this review is devoted to provide an overview on different established multienzymatic cascades for the production of non-canonical D-α-and L-α-AAs, supplying neophyte and experienced professionals in this field with different illustrative examples in the literature. Whereas the discovery of new or newly designed enzymes is of great interest, dusting off previous enzymatic methodologies by a "back and to the future" strategy might accelerate the implementation of new or improved multienzymatic cascades.

show abstract

“…Mutants in INS also showed changes in substrate spectrum and regulation of the L-AAD substrate preference. Therefore, INS plays a significant role in L-AAD structure and catalysis, but there are few researches in the modification of INS to improve the catalytic properties (Asano and Yasukawa, 2019).…”

Section: Introductionmentioning

confidence: 99%

Semi-rational engineering membrane binding domain of L-amino acid deaminase from Proteus vulgaris for enhanced α-ketoisocaproate

Song

Wang²,

Zhang³

et al. 2022

Front. Microbiol.

View full text Add to dashboard Cite

α-Keto acids are important raw materials for pharmaceuticals and functional foods, which could be produced from cheap feed stock by whole cell biocatalysts containing L-amino acid deaminases (L-AADs). However, the production capacity is limited by the low activity of L-AADs. The L-AAD mediated redox reaction employs the electron transport chain to transfer electrons from the reduced FADH2 to O2, implying that the interaction between L-AAD and the cell membrane affects its catalytic activity. To improve the catalytic activity of L-AAD from Proteus vulgaris, we redesigned the membrane-bound hydrophobic insertion sequences (INS, residues 325–375) by saturation mutagenesis and high-throughput screening. Mutants D340N and L363N exhibited higher affinity and catalytic efficiency for L-leucine, with half-life 1.62-fold and 1.28-fold longer than that of wild-type L-AAD. D340N catalyzed L-leucine to produce 81.21 g⋅L–1 α-ketoisocaproate, with a bioconversion rate of 89.06%, which was 17.57% higher than that of the wild-type. It is predicted that the mutations enhanced the interaction between the protein and the cell membrane.

show abstract

Identification and development of amino acid oxidases

Cited by 23 publications

References 49 publications

Оксидази L-Амінокислот: Одержання, Властивості Та Перспективи Використання

Оксидази L-Амінокислот: Одержання, Властивості Та Перспективи Використання

Overview on Multienzymatic Cascades for the Production of Non-canonical α-Amino Acids

Semi-rational engineering membrane binding domain of L-amino acid deaminase from Proteus vulgaris for enhanced α-ketoisocaproate

Contact Info

Product

Resources

About