QM/MM studies on the calcium-assisted β-elimination mechanism of pectate lyase from bacillus subtilis

2016 ◽  
Vol 84 (11) ◽  
pp. 1606-1615 ◽  
Author(s):  
Guangcai Ma ◽  
Wenyou Zhu ◽  
Yongjun Liu
Keyword(s):  
Bacillus Subtilis ◽  
Pectate Lyase ◽  
Elimination Mechanism

scholarly journals Pectate lyase C from Bacillus subtilis: a novel endo-cleaving enzyme with activity on highly methylated pectin

Microbiology ◽  
2006 ◽  
Vol 152 (3) ◽  
pp. 617-625 ◽  
Author(s):  
Margarita Soriano ◽  
Pilar Diaz ◽  
Francisco I. Javier Pastor
Keyword(s):  
Bacillus Subtilis ◽  
Pectate Lyase ◽  
Maximum Activity ◽  
Methyl Esterification ◽  
Pectate Lyases ◽  
Action Analysis ◽  
Paenibacillus Barcinonensis ◽  
Esterification Degree ◽  
Micro Organisms ◽  
High Degree

The gene yvpA from Bacillus subtilis was cloned and expressed in Escherichia coli. It encoded a pectate lyase of 221 amino acids that was denominated PelC. The heterologously expressed enzyme was purified by His-tag affinity chromatography and characterized. PelC depolymerized polygalacturonate and pectins of methyl esterification degree from 22 % to 89 %, exhibiting maximum activity on 22 % esterified citrus pectin. It showed an absolute Ca2+ requirement and the optimum temperature and pH were 65 °C and pH 10, respectively. The deduced amino acid sequence of PelC showed 53 % identity to pectate lyase PelA from Paenibacillus barcinonensis, which was also characterized. Similarly to PelC, purified PelA showed activity on polygalacturonate and pectins with a high degree of methyl esterification. The two enzymes cleaved pectic polymers to a mixture of oligogalacturonates, indicating an endo mode of action. Analysis of activity on trigalacturonate showed that PelC cleaved it to galacturonic acid and unsaturated digalacturonate, whereas PelA did not show activity on this substrate. PelC and PelA showed high homology to a few recently identified pectate lyases of family 3 and form with them a cluster of small-sized pectate lyases from non-pathogenic micro-organisms.

The purification and characterization of a novel alkali-stable pectate lyase produced by Bacillus subtilis PB1

2017 ◽  
Vol 33 (10) ◽  
Author(s):  
Man Zhou ◽  
Jingli Wu ◽  
Tao Wang ◽  
Lina Gao ◽  
Huijun Yin ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Pectate Lyase ◽  
Purification And Characterization

The structure of Bacillus subtilis pectate lyase in complex with calcium

1994 ◽  
Vol 1 (10) ◽  
pp. 717-723 ◽  
Author(s):  
Richard Pickersgill ◽  
John Jenkins ◽  
Gillian Harris ◽  
William Nasser ◽  
Janine Robert-Baudouy
Keyword(s):  
Bacillus Subtilis ◽  
Pectate Lyase

Purification and characterization of extracellular pectate lyase from Bacillus subtilis

Biochimie ◽  
1990 ◽  
Vol 72 (9) ◽  
pp. 689-695 ◽  
Author(s):  
W NASSER ◽  
F CHALET ◽  
J ROBERTBAUDOUY
Keyword(s):  
Bacillus Subtilis ◽  
Pectate Lyase ◽  
Purification And Characterization

Structural Insights into Substrate Specificity and theantiβ-Elimination Mechanism of Pectate Lyase

Biochemistry ◽  
2010 ◽  
Vol 49 (3) ◽  
pp. 539-546 ◽  
Author(s):  
Arefeh Seyedarabi ◽  
Teng Teng To ◽  
Salyha Ali ◽  
Syeed Hussain ◽  
Markus Fries ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Pectate Lyase ◽  
Elimination Mechanism ◽  
Structural Insights

Improving the specific activity and thermo-stability of alkaline pectate lyase from Bacillus subtilis 168 for bioscouring

2018 ◽  
Vol 129 ◽  
pp. 74-83 ◽  
Author(s):  
Xiaowen Wang ◽  
Zhenghui Lu ◽  
Ting Xu ◽  
Jonathan Nimal Selvaraj ◽  
Li Yi ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Specific Activity ◽  
Pectate Lyase ◽  
Bacillus Subtilis 168 ◽  
Alkaline Pectate Lyase ◽  
Thermo Stability

Crystallization and preliminary X-ray studies of the pectate lyase from Bacillus subtilis

1992 ◽  
Vol 228 (4) ◽  
pp. 1255-1258 ◽  
Author(s):  
John Jenkins ◽  
William Nasser ◽  
Mandy Scott ◽  
Richard Pickersgill ◽  
Jean-Charles Vignon ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Pectate Lyase ◽  
X Ray
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