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Pregled bibliografske jedinice broj: 1060248

Computational study of glycerol binding within the active site of coenzyme B12-dependent diol dehydratase


Bilić, Luka; Barić, Danijela; Banhatti, Radha Dilip; Smith, David Matthew; Kovačević, Borislav
Computational study of glycerol binding within the active site of coenzyme B12-dependent diol dehydratase // Computational Chemistry Day2019
Zagreb, Hrvatska, 2019. (poster, podatak o recenziji nije dostupan, neobjavljeni rad, znanstveni)


CROSBI ID: 1060248 Za ispravke kontaktirajte CROSBI podršku putem web obrasca

Naslov
Computational study of glycerol binding within the active site of coenzyme B12-dependent diol dehydratase

Autori
Bilić, Luka ; Barić, Danijela ; Banhatti, Radha Dilip ; Smith, David Matthew ; Kovačević, Borislav

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, neobjavljeni rad, znanstveni

Skup
Computational Chemistry Day2019

Mjesto i datum
Zagreb, Hrvatska, 11.05.2019

Vrsta sudjelovanja
Poster

Vrsta recenzije
Podatak o recenziji nije dostupan

Ključne riječi
B12-dependent diol dehydratase ; Substrate binding ; Glycerol inactivation ; Molecular dynamics ; QM/MM calculations

Sažetak
Microbial conversion of crude glycerol (GOL), waste from biofuel production, into compounds of greater industrial value could solve technical difficulties encountered by conventional means of chemical conversion [1]. During microbial conversion the first step GOL undergoes is dehydration by enzymes dehydratases into 3-hydroxylpropionaldehyde (3HPA) [2-3]. Two classes of dehydratases can catalyze dehydration of GOL, B12-independent and B12-dependent dehydratases, from which B12- dependent class is more often used due to its tolerance to aerobic conditions [4]. However, a peculiar property of B12-dependent dehydratases is that the substrate GOL also acts as an irreversible inhibitor [5]. Based on the B12- dependent diol dehydratase (B12-dDDH) crystal structure with GOL (PDB code: 3AUJ) K.Yoshizawa et.al. concluded that the geometry of such bound GOL enables radical reorganization causing inhibition [6]. However, in the recent study on similar enzyme B12-dependent glycerol dehydratase employing classical molecular dynamics we observed GOL in a different geometry [7]. Here we present a detailed study of the GOL geometries within the active site of B12-dDDH and consider implications of our findings for the mechanism of substrate induced inactivation.

Izvorni jezik
Engleski

Znanstvena područja
Kemija



POVEZANOST RADA


Projekti:
HRZZ-IP-2013-11-8238 - Računalna rješenja u bioznanostima: Značaj savitljivosti molekula (CompSoLS-MolFlex) (Matthew Smith, David, HRZZ - 2013-11) ( POIROT)

Ustanove:
Institut "Ruđer Bošković", Zagreb


Citiraj ovu publikaciju

Bilić, Luka; Barić, Danijela; Banhatti, Radha Dilip; Smith, David Matthew; Kovačević, Borislav
Computational study of glycerol binding within the active site of coenzyme B12-dependent diol dehydratase // Computational Chemistry Day2019
Zagreb, Hrvatska, 2019. (poster, podatak o recenziji nije dostupan, neobjavljeni rad, znanstveni)
Bilić, L., Barić, D., Banhatti, R., Smith, D. & Kovačević, B. (2019) Computational study of glycerol binding within the active site of coenzyme B12-dependent diol dehydratase. U: Computational Chemistry Day2019.
@article{article, year = {2019}, keywords = {B12-dependent diol dehydratase, Substrate binding, Glycerol inactivation, Molecular dynamics, QM/MM calculations}, title = {Computational study of glycerol binding within the active site of coenzyme B12-dependent diol dehydratase}, keyword = {B12-dependent diol dehydratase, Substrate binding, Glycerol inactivation, Molecular dynamics, QM/MM calculations}, publisherplace = {Zagreb, Hrvatska} }
@article{article, year = {2019}, keywords = {B12-dependent diol dehydratase, Substrate binding, Glycerol inactivation, Molecular dynamics, QM/MM calculations}, title = {Computational study of glycerol binding within the active site of coenzyme B12-dependent diol dehydratase}, keyword = {B12-dependent diol dehydratase, Substrate binding, Glycerol inactivation, Molecular dynamics, QM/MM calculations}, publisherplace = {Zagreb, Hrvatska} }




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