An enzymatic complex active in sulphite and thiosulphate oxidation by Rhodotorula sp.

1983 ◽  
Vol 134 (2) ◽  
pp. 143-147 ◽  
Author(s):  
Ewa J. Kurek
Author(s):  
L.S. Martins ◽  
E.E.L. Valente ◽  
F.A.P. Santos ◽  
O.F. Stuani ◽  
L.S. Leite ◽  
...  

2020 ◽  
Author(s):  
Michal Lisnyansky Bar-El ◽  
Pavla Vankova ◽  
Petr Man ◽  
Yoni Haitin ◽  
Moshe Giladi

AbstractThe human cis-prenyltransferase (hcis-PT) is an enzymatic complex essential for protein N-glycosylation. Synthesizing the precursor of the glycosyl carrier dolichol-phosphate, we reveal here that hcis-PT exhibits a novel heterotetrameric assembly in solution, composed of two catalytic dehydrodolichyl diphosphate synthase (DHDDS) and two inactive Nogo-B receptor (NgBR) subunits. The 2.3 Å crystal structure of the complex exposes a dimer-of-heterodimers arrangement, with DHDDS C-termini serving as homotypic assembly domains. Furthermore, the structure elucidates the molecular details associated with substrate binding, catalysis, and product length determination. Importantly, the distal C-terminus of NgBR transverses across the heterodimeric interface, directly participating in substrate binding and underlying the allosteric communication between the subunits. Finally, mapping disease-associated hcis-PT mutations involved in blindness, neurological and glycosylation disorders onto the structure reveals their clustering around the active site. Together, our structure of the hcis-PT complex unveils the dolichol synthesis mechanism and its perturbation in disease.


2016 ◽  
Vol 30 (3) ◽  
pp. 410-416 ◽  
Author(s):  
Eveline Berwanger ◽  
Ricardo Vianna Nunes ◽  
Tiago Junior Pasquetti ◽  
Alice Eiko Murakami ◽  
Taciana Maria Moraes de Oliveira ◽  
...  

2018 ◽  
Vol 18 (9) ◽  
pp. 692-701 ◽  
Author(s):  
Ekaterina Krumova ◽  
Nedelina Kostadinova ◽  
Jeni Miteva-Staleva ◽  
Galina Stoyancheva ◽  
Boryana Spassova ◽  
...  

1964 ◽  
Vol 17 (2) ◽  
pp. 577 ◽  
Author(s):  
PA Trudinger

The autotrophic bacteria, Thiobacillus spp., oxidize thiosulphate to sulphate but the mechanism of this reaction is obscure (see Vishniac and Trodinger 1962). The suggestion that tetrathionate is an intermediate (Tamiya, Raga, and Huzisige 1941; Vishniac and Santer 1957; Jones and Happold 1961) has been contested by Ostrowski and Krawczyk (1957) and by Peck (1960), who have proposed that a scission of the thiosulphate molecule takes place prior to oxidation.


2016 ◽  
Vol 15 (6) ◽  
pp. 78-83
Author(s):  
A. P. Sinitsyn ◽  
O. G. Korotkova ◽  
O. A. Sinitsyna ◽  
A. M. Rozhkova ◽  
G. S. Dotsenko ◽  
...  

2010 ◽  
Vol 19 (5) ◽  
pp. 1387-1390 ◽  
Author(s):  
Juan Buenrostro-Figueroa ◽  
Heliodoro de la Garza-Toledo ◽  
Vrani Ibarra-Junquera ◽  
Cristóbal Noe Aguilar

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