scholarly journals Phosphomimetic T335D Mutation of Hydroxypyruvate Reductase 1 Modifies Cofactor Specificity and Impacts Arabidopsis Growth in Air

2020 ◽  
Vol 183 (1) ◽  
pp. 194-205 ◽  
Author(s):  
Yanpei Liu ◽  
Florence Guérard ◽  
Michael Hodges ◽  
Mathieu Jossier
Keyword(s):  
Cofactor Specificity ◽  
Hydroxypyruvate Reductase

scholarly journals Exploration of the cofactor specificity of wild-type phosphite dehydrogenase and its mutant using molecular dynamics simulations

RSC Advances ◽  
2021 ◽  
Vol 11 (24) ◽  
pp. 14527-14533
Author(s):  
Kunlu Liu ◽  
Min Wang ◽  
Yubo Zhou ◽  
Hongxiang Wang ◽  
Yudong Liu ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulations ◽  
Wild Type ◽  
Cofactor Specificity ◽  
Phosphite Dehydrogenase ◽  
Dynamics Simulations

Phosphite dehydrogenase (Pdh) catalyzes the NAD-dependent oxidation of phosphite to phosphate with the formation of NADH.

scholarly journals A DNA Ligase from a Hyperthermophilic Archaeon with Unique Cofactor Specificity

2000 ◽  
Vol 182 (22) ◽  
pp. 6424-6433 ◽  
Author(s):  
Masaru Nakatani ◽  
Satoshi Ezaki ◽  
Haruyuki Atomi ◽  
Tadayuki Imanaka
Keyword(s):  
Biochemical Study ◽  
Protein Product ◽  
Optimum Concentration ◽  
Dna Ligase ◽  
Gene Encoding ◽  
Hyperthermophilic Archaeon ◽  
Dna Ligases ◽  
Cofactor Specificity ◽  
Thermophilic Archaeon ◽  
Optimum Ph

ABSTRACT A gene encoding DNA ligase (ligTk ) from a hyperthermophilic archaeon, Thermococcus kodakaraensisKOD1, has been cloned and sequenced, and its protein product has been characterized. ligTk consists of 1,686 bp, corresponding to a polypeptide of 562 amino acids with a predicted molecular mass of 64,079 Da. Sequence comparison with previously reported DNA ligases and the presence of conserved motifs suggested that Lig Tk was an ATP-dependent DNA ligase. Phylogenetic analysis indicated that Lig Tk was closely related to the ATP-dependent DNA ligase fromMethanobacterium thermoautotrophicum ΔH, a moderate thermophilic archaeon, along with putative DNA ligases fromEuryarchaeota and Crenarchaeota. We expressedligTk in Escherichia coli and purified the recombinant protein. Recombinant Lig Tk was monomeric, as is the case for other DNA ligases. The protein displayed DNA ligase activity in the presence of ATP and Mg2+. The optimum pH of Lig Tk was 8.0, the optimum concentration of Mg2+, which was indispensable for the enzyme activity, was 14 to 18 mM, and the optimum concentration of K+ was 10 to 30 mM. Lig Tk did not display single-stranded DNA ligase activity. At enzyme concentrations of 200 nM, we observed significant DNA ligase activity even at 100°C. Unexpectedly, Lig Tk displayed a relatively small, but significant, DNA ligase activity when NAD+ was added as the cofactor. Treatment of NAD+ with hexokinase did not affect this activity, excluding the possibility of contaminant ATP in the NAD+ solution. This unique cofactor specificity was also supported by the observation of adenylation of Lig Tk with NAD+. This is the first biochemical study of a DNA ligase from a hyperthermophilic archaeon.

Role of aspartate-37 in determining cofactor specificity and binding in rat liver dihydropteridine reductase

1991 ◽  
Vol 287 (1) ◽  
pp. 234-239 ◽  
Author(s):  
D.A. Matthews ◽  
K.I. Varughese ◽  
M. Skinner ◽  
N.H. Xuong ◽  
J. Hoch ◽  
...  
Keyword(s):  
Rat Liver ◽  
Dihydropteridine Reductase ◽  
Cofactor Specificity

Crystallization and preliminary diffraction studies of hydroxypyruvate reductase (d-glycerate dehydrogenase) from Hyphomicrobium methylovorum

1992 ◽  
Vol 225 (3) ◽  
pp. 909-911 ◽  
Author(s):  
Jonathan D. Goldberg ◽  
Peter Brick ◽  
Toyokazu Yoshida ◽  
Toshio Mitsunaga ◽  
Takashi Oshiro ◽  
...  
Keyword(s):  
Hydroxypyruvate Reductase
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