Self-sufficient cytochrome P450 monooxygenases from Bacillus thuringiensis: amplification and comparative sequence analysis

Biologija ◽  
2008 ◽  
Vol 54 (3) ◽  
pp. 187-191
Author(s):  
Romualdas Griškevičius ◽  
Nomeda Kuisienė ◽  
Juozas Raugalas ◽  
Džiuginta Jasinskytė ◽  
Donaldas Čitavičius
1984 ◽  
Vol 51 (1) ◽  
pp. 97-101 ◽  
Author(s):  
G W Both ◽  
L J Siegman ◽  
A R Bellamy ◽  
N Ikegami ◽  
A J Shatkin ◽  
...  

Toxicology ◽  
1994 ◽  
Vol 93 (2-3) ◽  
pp. 165-173 ◽  
Author(s):  
Morio Fukuhara ◽  
Eric Antignac ◽  
Naomi Fukusen ◽  
Kazue Kato ◽  
Masanobu Kimura

PLoS ONE ◽  
2017 ◽  
Vol 12 (6) ◽  
pp. e0178829 ◽  
Author(s):  
Wander de Jesus Jeremias ◽  
Flávio Marcos Gomes Araújo ◽  
Fábio Ribeiro Queiroz ◽  
Fabiano Sviatopolk Mirsky Pais ◽  
Ana Carolina Alves de Mattos ◽  
...  

1987 ◽  
Vol 262 (24) ◽  
pp. 11794-11800 ◽  
Author(s):  
K D Cole ◽  
G P Fernando-Warnakulasuriya ◽  
M S Boguski ◽  
M Freeman ◽  
J I Gordon ◽  
...  

2018 ◽  
Vol 475 (23) ◽  
pp. 3875-3886 ◽  
Author(s):  
Craig S. Robb ◽  
Lukas Reisky ◽  
Uwe T. Bornscheuer ◽  
Jan-Hendrik Hehemann

Degradation of carbohydrates by bacteria represents a key step in energy metabolism that can be inhibited by methylated sugars. Removal of methyl groups, which is critical for further processing, poses a biocatalytic challenge because enzymes need to overcome a high energy barrier. Our structural and computational analysis revealed how a member of the cytochrome P450 family evolved to oxidize a carbohydrate ligand. Using structural biology, we ascertained the molecular determinants of substrate specificity and revealed a highly specialized active site complementary to the substrate chemistry. Invariance of the residues involved in substrate recognition across the subfamily suggests that they are critical for enzyme function and when mutated, the enzyme lost substrate recognition. The structure of a carbohydrate-active P450 adds mechanistic insight into monooxygenase action on a methylated monosaccharide and reveals the broad conservation of the active site machinery across the subfamily.


2004 ◽  
Vol 135 (1) ◽  
pp. 459-470 ◽  
Author(s):  
Yong Qiang Gu ◽  
Devin Coleman-Derr ◽  
Xiuying Kong ◽  
Olin D. Anderson

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