SASDET5: Old Yellow Enzyme of Leishmania braziliensis (LbOYE)

Basic information

• Entry: Database: SASBDB / ID: SASDET5

Sample

Old Yellow Enzyme of Leishmania braziliensis

• Old Yellow Enzyme of Leishmania braziliensis (protein), LbOYE, Leishmania braziliensis

• Biological species: Leishmania braziliensis (eukaryote)
• Citation: Journal: Arch Biochem Biophys / Year: 2019; Title: Structural studies of Old Yellow Enzyme of Leishmania braziliensis in solution.; Authors: Laudimir Leonardo Walbert Veloso-Silva / Paulo Roberto Dores-Silva / Dayane Eliara Bertolino-Reis / Louis Fellipe Moreno-Oliveira / Silvia Helena Libardi / Júlio César Borges / ; Abstract: First described in yeast in 1932 by Christian & Warburg, the Old Yellow Enzyme (OYE) (EC 1.6.99.1) has aroused the interest of the scientific community regarding its high ability to catalyze stereoselective reactions of α/β-unsaturated carbonyl compounds with important industrial applications. In addition, the OYE family of proteins has been found in different organisms, such as plants, bacteria and protozoa, but not in mammals, which makes it an excellent candidate for a functional and molecular study aimed at more effective therapies with fewer undesirable side effects. Several OYE orthologues have been characterized; however, the real physiological role for most members of this family of proteins remains a mystery. In this paper, we present the structural studies of the OYE of Leishmania braziliensis. The findings are discussed in comparison with OYE of Trypanosoma cruzi, revealing some biophysical differences. The main differences are related to their chemical and thermal stabilities and behavior in solution. In addition, the L. braziliensis OYE shape is more elongated than that of the T. cruzi orthologue. Despite this, the active sites of these enzymes do not appear to have major differences, since their interactions with the substrate menadione occur with an affinity of the same order of magnitude, revealing that the binding sites in both proteins are essentially similar.

Contact author

• Júlio Borges (Instituto de Química de São Carlos, São Carlos - SP - Brasil)

Models

• Model #2480: ; Type: dummy / Radius of dummy atoms: 2.40 A / Chi-square value: 6.159; Search similar-shape structures of this assembly by Omokage search (details)

Sample

• Sample: Name: Old Yellow Enzyme of Leishmania braziliensis / Specimen concentration: 3 mg/ml
• Buffer: Name: 25 mM Tris-HCl 100 mM NaCl and 1 mM β-mercaptoethanol; pH: 8

Entity #1325

Name: LbOYE / Type: protein / Description: Old Yellow Enzyme of Leishmania braziliensis / Formula weight: 41.859 / Num. of mol.: 1 / Source: Leishmania braziliensis
Sequence:

GSEFDYTMPT ASNSIDALLK PLVIGQLSMP NRFVMAPLTR CRADDEHVPT PAMVRHYADR ASMGLIITEA TQIEKGYSTF CHEGGIYGKE QVDGWRKVTD AVHEKGGLIF CQIHNGGRAT VPSNVDEGVR IVAPSAVAIT DHECPGAFAR NGEKQPYPVP HEMTAEDIAL YVKLYATAAC NAMAAGFDGV EVHGANGYLI DEFLKSSSNQ RTDEYGGSIE NRCRFLFEVL DAVIKAIGRE RVGLRISPLN SFNSQSDENP EALTRYICSQ LNSRNISFLD VMRGDFFSQA CGADKWAREA YEGVLFTGMG FEIEEAAETV ASGAADAVVF GTKALANPDL VARAIAGAAL NTPDPATFYS TSEAGYNDYP SMVSSCPSAA APSCTKETP

Experimental information

• Beam: Instrument name: Brazilian Synchrotron Light Laboratory SAXS1 Beamline; City: Campinas / 国: Brazil / Type of source: X-ray synchrotron / Wavelength: 0.148 Å / Dist. spec. to detc.: 1 mm
• Detector: Name: Pilatus 300K / Type: 20Hz

Scan

Title: Old Yellow Enzyme of Leishmania braziliensis / Measurement date: May 26, 2015 / Storage temperature: 4 °C / Cell temperature: 25 °C / Exposure time: 360 sec. / Number of frames: 1 / Unit: 1/A /

	Min	Max
Q	0.0234	0.3181

Distance distribution function P(R)

Sofotware P(R): GNOM 4.6 / Number of points: 234 /

	Min	Max
Q	0.02344	0.3181
P(R) point	1	234
R	0	108

Result

Type of curve: single_conc

	Experimental	Standard	Standard error	Porod
MW	40 kDa	48.6 kDa	4	40 kDa
Volume	-	-	-	73 nm3

	P(R)	P(R) error	Guinier	Guinier error
Forward scattering, I0	0.3768	0.037	0.381	0.0007
Radius of gyration, Rg	2.69 nm	0.2	2.71 nm	-

	Min	Max	Error
D	-	9.5	1
Guinier point	1	16	-