scholarly journals Crystal structure of NAD+-dependent Peptoniphilus asaccharolyticus glutamate dehydrogenase reveals determinants of cofactor specificity

2012 ◽  
Vol 177 (2) ◽  
pp. 543-552 ◽  
Author(s):  
Tânia Oliveira ◽  
Santosh Panjikar ◽  
John B. Carrigan ◽  
Muaawia Hamza ◽  
Michael A. Sharkey ◽  
...  
Author(s):  
Tânia Oliveira ◽  
Michael A. Sharkey ◽  
Paul C. Engel ◽  
Amir R. Khan

Glutamate dehydrogenases (EC 1.4.1.2–4) catalyse the oxidative deamination of L-glutamate to α-ketoglutarate using NAD(P)+as a cofactor. The bacterial enzymes are hexameric, arranged with 32 symmetry, and each polypeptide consists of an N-terminal substrate-binding segment (domain I) followed by a C-terminal cofactor-binding segment (domain II). The catalytic reaction takes place in the cleft formed at the junction of the two domains. Distinct signature sequences in the nucleotide-binding domain have been linked to the binding of NAD+versusNADP+, but they are not unambiguous predictors of cofactor preference. In the absence of substrate, the two domains move apart as rigid bodies, as shown by the apo structure of glutamate dehydrogenase fromClostridium symbiosum. Here, the crystal structure of a chimaeric clostridial/Escherichia colienzyme has been determined in the apo state. The enzyme is fully functional and reveals possible determinants of interdomain flexibility at a hinge region following the pivot helix. The enzyme retains the preference for NADP+cofactor from the parentE. colidomain II, although there are subtle differences in catalytic activity.


2021 ◽  
Author(s):  
Christina Dimovasili ◽  
Vasiliki E. Fadouloglou ◽  
Aikaterini Kefala ◽  
Mary Providaki ◽  
Dina Kotsifaki ◽  
...  

2021 ◽  
Vol 570 ◽  
pp. 15-20
Author(s):  
Na Li ◽  
Wenfeng Wang ◽  
Xue Zeng ◽  
Mingjie Liu ◽  
Mengyu Li ◽  
...  

FEBS Letters ◽  
2017 ◽  
Vol 591 (11) ◽  
pp. 1611-1622 ◽  
Author(s):  
Takeo Tomita ◽  
Lulu Yin ◽  
Shugo Nakamura ◽  
Saori Kosono ◽  
Tomohisa Kuzuyama ◽  
...  

2005 ◽  
Vol 345 (2) ◽  
pp. 325-337 ◽  
Author(s):  
Mohammad W. Bhuiya ◽  
Haruhiko Sakuraba ◽  
Toshihisa Ohshima ◽  
Takahito Imagawa ◽  
Nobuhiko Katunuma ◽  
...  

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