Structure of a soluble epoxide hydrolase identified in Trichoderma reesei

Wilson, Carolina; Oliveira, Gabriel Stephani de; Adriani, P.P.; Chambergo, Felipe S.; Dias, Marcio V.B.

doi:10.1016/j.bbapap.2017.05.004

Cited by 10 publications

(12 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Nevertheless, the LEH from pQR1982 had comparable temperature tolerance to the reported LEHs. The ⍺/β EH from pQR1984 had a temperature optimum of 30 °C which is within the typical reported temperature range of 15−50 °C for ⍺/β EHs [ 32 , 41 ]. To determine if lower enzyme and higher substrate concentrations could be used, the enzyme concentration was reduced to 0.1 mg/mL from 0.4 mg/mL and rac - 1a was added at concentrations of 1 mM – 50 mM.…”

Section: Resultssupporting

confidence: 74%

“…These were passed into the ClustalOmega web service to generate a percentage identity matrix, which was visualised in Python 3 using the seaborn package. Twenty-six of the ⍺/β EH sequences were grouped with 185 ⍺/β EHs sequences from [ 24 ] and [ 20 ] sequences of literature reported ⍺/β EHs [ 11 , 13 , 17 , 18 , 24 , 25 , [31] , [32] , [33] , [34] , [35] ]. Similarly the three LEH sequences were grouped with six literature reported LEHs [ 7 , 9 , 10 , 36 ].…”

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Identification and catalytic properties of new epoxide hydrolases from the genomic data of soil bacteria

Stojanovski

Dobrijevic

Hailes

et al. 2020

Enzyme and Microbial Technology

View full text Add to dashboard Cite

Highlights Five new active epoxide hydrolases were found. The limonene epoxide hydrolase from pQR1982 has a wide substrate scope. Enzymes from pQR1982 and pQR1984 had opposite epoxide ring-opening stereoselectivities. Enzymes from pQR1984 and pQR1990 de-symmetrised the meso -epoxide, cyclohexene oxide. The ⍺/β EH from pQR1984 had comparable activity in the presence of 5–30% MeOH.

show abstract

Section: Resultssupporting

confidence: 74%

Section: Methodsmentioning

confidence: 99%

Identification and catalytic properties of new epoxide hydrolases from the genomic data of soil bacteria

Stojanovski

Dobrijevic

Hailes

et al. 2020

Enzyme and Microbial Technology

View full text Add to dashboard Cite

show abstract

“…for superposition of the three different protomers in the asymmetric unit is about 0.3 Å , indicating that they are very similar and there are no large conformation changes between them. This is, at least to our knowledge, the first description of a hexameric soluble epoxide hydrolase, in contrast to several dimeric soluble EHs (Mowbray et al, 2006;Gomez et al, 2004;James et al, 2008;Argiriadi et al, 1999) and a monomeric soluble EH characterized by our research group (Wilson et al, 2017;de Oliveira, Adriani et al, 2019). The hexamer is stabilized predominantly by hydrophobic interactions, with similar interaction surfaces of 724 and 708 Å 2 between protomers A and B and protomers B and C, respectively, and with a further nine and 14 ionic interactions observed between protomers A and B and protomers B and C, respectively ( Supplementary Fig.…”

Section: Structure Of B1eph2mentioning

confidence: 60%

An epoxide hydrolase from endophyticStreptomycesshows unique structural features and wide biocatalytic activity

Tormet‐González

Wilson

Oliveira

et al. 2020

Acta Cryst Sect D Struct Biol

Self Cite

View full text Add to dashboard Cite

The genus Streptomyces is characterized by the production of a wide variety of secondary metabolites with remarkable biological activities and broad antibiotic capabilities. The presence of an unprecedented number of genes encoding hydrolytic enzymes with industrial appeal such as epoxide hydrolases (EHs) reveals its resourceful microscopic machinery. The whole-genome sequence of Streptomyces sp. CBMAI 2042, an endophytic actinobacterium isolated from Citrus sinensis branches, was explored by genome mining, and a putative α/β-epoxide hydrolase named B1EPH2 and encoded by 344 amino acids was selected for functional and structural studies. The crystal structure of B1EPH2 was obtained at a resolution of 2.2 Å and it was found to have a similar fold to other EHs, despite its hexameric quaternary structure, which contrasts with previously solved dimeric and monomeric EH structures. While B1EPH2 has a high sequence similarity to EHB from Mycobacterium tuberculosis, its cavity is similar to that of human EH. A group of 12 aromatic and aliphatic racemic epoxides were assayed to determine the activity of B1EPH2; remarkably, this enzyme was able to hydrolyse all the epoxides to the respective 1,2-diols, indicating a wide-range substrate scope acceptance. Moreover, the (R)- and (S)-enantiomers of styrene oxide, epichlorohydrin and 1,2-epoxybutane were used to monitor enantiopreference. Taken together, the functional and structural analyses indicate that this enzyme is an attractive biocatalyst for future biotechnological applications.

show abstract

“…Recently, our group reported the 3D-structure of a soluble EH from Trichoderma reesei QM9414 (TrEH) [16] and we also have identified potent and effective inhibitors against this enzyme (figure 1, compounds 2-5). In addition, these compounds inhibited the fungal growth in more than 60% [17].…”

Section: Introductionmentioning

confidence: 99%

The molecular structure of an epoxide hydrolase from Trichoderma reesei in complex with urea or amide-based inhibitors

Oliveira

Adriani

Ribeiro

et al. 2019

International Journal of Biological Macromolecules

Self Cite

View full text Add to dashboard Cite

Epoxide hydrolases (EHs) are enzymes involved in the metabolism of endogenous and exogenous epoxides, and the development of EH inhibitors has important applications in the medicine. In humans, EH inhibitors are being tested in the treatment of cardiovascular diseases and show potent anti-inflammatory effects. EH inhibitors are also considerate promising molecules against infectious diseases. EHs are functionally very well studied, but only a few members have its threedimensional structures characterized. Recently, a new EH from the filamentous fungi Trichoderma reseei (TrEH) was reported, and a series of urea or amide-based inhibitors were identified. In this study, we describe the crystallographic structures of TrEH in complex with five different urea or amide-based inhibitors with resolutions ranging from 2.6 to 1.7 Å. The analysis of these structures reveals the molecular basis of the inhibition of these compounds. We could also observe that these inhibitors occupy the whole extension of the active site groove and only a few conformational changes are involved. Understanding the structural basis EH interactions with different inhibitors might substantially contribute for the study of fungal metabolism and in the development of novel and more efficient antifungal drugs against pathogenic Trichoderma species.

show abstract

Structure of a soluble epoxide hydrolase identified in Trichoderma reesei

Cited by 10 publications

References 42 publications

Identification and catalytic properties of new epoxide hydrolases from the genomic data of soil bacteria

Identification and catalytic properties of new epoxide hydrolases from the genomic data of soil bacteria

An epoxide hydrolase from endophyticStreptomycesshows unique structural features and wide biocatalytic activity

The molecular structure of an epoxide hydrolase from Trichoderma reesei in complex with urea or amide-based inhibitors

Contact Info

Product

Resources

About