Structural insight into the catalytic mechanism of a cis-epoxysuccinate hydrolase producing enantiomerically pure d(−)-tartaric acid

2018 ◽  
Vol 54 (61) ◽  
pp. 8482-8485 ◽  
Author(s):  
Sheng Dong ◽  
Xi Liu ◽  
Gu-Zhen Cui ◽  
Qiu Cui ◽  
Xinquan Wang ◽  
...  
Keyword(s):  
Tartaric Acid ◽  
Catalytic Mechanism ◽  
Enantiomerically Pure ◽  
Tartaric Acids ◽  
Structural Insight ◽  
Insight Into ◽  
High Stereoselectivity

The catalytic mechanism for the high stereoselectivity and product enantioselectivity of a cis-epoxysuccinate hydrolase producing d(−)-tartaric acids was elucidated.

scholarly journals Structural studies on dehydroshikimate dehydratase

2014 ◽  
Vol 70 (a1) ◽  
pp. C475-C475
Author(s):  
James Peek ◽  
Dinesh Christendat
Keyword(s):  
Sole Carbon Source ◽  
Catalytic Mechanism ◽  
Substrate Recognition ◽  
Structural Studies ◽  
Sugar Phosphate ◽  
X Ray ◽  
Structural Insight ◽  
Functional Relevance ◽  
Insight Into

The soil bacterium, Pseudomonas putida, is capable of using the alicyclic compound quinate as a sole carbon source. During this process, quinate is converted to 3-dehydroshikimate, which subsequently undergoes a dehydration to form protocatechuate. The latter transformation is performed by the enzyme dehydroshikimate dehydratase (DSD). We have recombinantly produced DSD from P. putida and are currently performing x-ray crystallographic studies on the enzyme to gain structural insight into its catalytic mechanism and mode of substrate recognition. Initial crystals of DSD diffracted to 2.7 Ä resolution, but exhibited strong twinning. A redesigned construct has recently yielded crystals that diffract to similar resolution, but with a significantly reduced tendency toward twinning. Interestingly, sequence analysis of P. putida DSD reveals that the protein is in fact a fusion of two distinct domains: an N-terminal sugar phosphate isomerase-like domain associated with DSD activity, and a C-terminal hydroxyphenylpyruvate dioxygenase (HPPD)-like domain with unknown functional significance. Structural characterization of the protein may provide novel insight into the functional relevance of the unusual HPPD-like domain.

scholarly journals Structural insight into poly(A) binding and catalytic mechanism of human PARN

2005 ◽  
Vol 24 (23) ◽  
pp. 4082-4093 ◽  
Author(s):  
Mousheng Wu ◽  
Michael Reuter ◽  
Hauke Lilie ◽  
Yuying Liu ◽  
Elmar Wahle ◽  
...  
Keyword(s):  
Catalytic Mechanism ◽  
Structural Insight ◽  
Insight Into

scholarly journals Structural insight into catalytic mechanism of PET hydrolase

2017 ◽  
Vol 8 (1) ◽  
Author(s):  
Xu Han ◽  
Weidong Liu ◽  
Jian-Wen Huang ◽  
Jiantao Ma ◽  
Yingying Zheng ◽  
...  
Keyword(s):  
Catalytic Mechanism ◽  
Structural Insight ◽  
Insight Into ◽  
Pet Hydrolase

Structural Insight into the Catalytic Mechanism of the Endoperoxide Synthase FtmOx1

2021 ◽  
Author(s):  
Jiahai Zhou ◽  
Lian Wu ◽  
Zhanfeng Wang ◽  
Yixin Cen ◽  
Binju Wang
Keyword(s):  
Catalytic Mechanism ◽  
Structural Insight ◽  
Insight Into

Copper–oxygen Dynamics in Tyrosinase

2019 ◽  
Author(s):  
Nobutaka Fujieda ◽  
Sachiko Yanagisawa ◽  
Minoru Kubo ◽  
Genji Kurisu ◽  
Shinobu Itoh
Keyword(s):  
Catalytic Mechanism ◽  
Substrate Binding ◽  
Active Form ◽  
Copper Ion ◽  
Atomic Resolution ◽  
Oxygen Species ◽  
X Ray ◽  
Oxygen Dynamics ◽  
Insight Into ◽  
Copper Centre

To unveil the activation of dioxygen on the copper centre (Cu<sub>2</sub>O<sub>2</sub>core) of tyrosinase, we performed X-ray crystallograpy with active-form tyrosinase at near atomic resolution. This study provided a novel insight into the catalytic mechanism of the tyrosinase, including the rearrangement of copper-oxygen species as well as the intramolecular migration of copper ion induced by substrate-binding.<br>

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