scholarly journals Molecular and Biochemical Characterization of Three WD-Repeat-Domain-containing Inositol Polyphosphate 5-Phosphatases in Arabidopsis thaliana

2004 ◽  
Vol 45 (11) ◽  
pp. 1720-1728 ◽  
Author(s):  
Ruiqin Zhong ◽  
Zheng-Hua Ye
Keyword(s):  
Arabidopsis Thaliana ◽  
Biochemical Characterization ◽  
Inositol Polyphosphate ◽  
Repeat Domain ◽  
Wd Repeat

scholarly journals Molecular and Biochemical Characterization of Two Plant Inositol Polyphosphate 6-/3-/5-Kinases

2002 ◽  
Vol 277 (45) ◽  
pp. 42711-42718 ◽  
Author(s):  
Jill Stevenson-Paulik ◽  
Audrey R. Odom ◽  
John D. York
Keyword(s):  
Biochemical Characterization ◽  
Inositol Polyphosphate

scholarly journals Biochemical characterization of the novel endo -β-mannanase At Man5-2 from Arabidopsis thaliana

Plant Science ◽  
2015 ◽  
Vol 241 ◽  
pp. 151-163 ◽  
Author(s):  
Yang Wang ◽  
Shoaib Azhar ◽  
Rosaria Gandini ◽  
Christina Divne ◽  
Ines Ezcurra ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Biochemical Characterization ◽  
The Novel

scholarly journals Functional and biochemical characterization of a recombinant Arabidopsis thaliana 3-deoxy-D-manno-octulosonate 8-phosphate synthase

2004 ◽  
Vol 381 (1) ◽  
pp. 185-193 ◽  
Author(s):  
Jing WU ◽  
Mayur A. PATEL ◽  
Appavu K. SUNDARAM ◽  
Ronald W. WOODARD
Keyword(s):  
Arabidopsis Thaliana ◽  
Molecular Mass ◽  
Biochemical Characterization ◽  
Dipicolinic Acid ◽  
Kinetic Studies ◽  
Maximum Activity ◽  
Reading Frame ◽  
Sequential Mechanism ◽  
Phosphate Synthase

An open reading frame, encoding for KDOPS (3-deoxy-D-manno-octulosonate 8-phosphate synthase), from Arabidopsis thaliana was cloned into a T7-driven expression vector. The protein was overexpressed in Escherichia coli and purified to homogeneity. Recombinant A. thaliana KDOPS, in solution, displays an apparent molecular mass of 76 kDa and a subunit molecular mass of 31.519 kDa. Unlike previously studied bacterial KDOPSs, which are tetrameric, A. thaliana KDOPS appears to be a dimer in solution. The optimum temperature of the enzyme is 65 °C and the optimum pH is 7.5, with a broad peak between pH 6.5 and 9.5 showing 90% of maximum activity. The enzyme cannot be inactivated by EDTA or dipicolinic acid treatment, nor it can be activated by a series of bivalent metal ions, suggesting that it is a non-metallo-enzyme, as opposed to the initial prediction that it would be a metallo-enzyme. Kinetic studies showed that the enzyme follows a sequential mechanism with Km=3.6 μM for phosphoenolpyruvate and 3.8 μM for D-arabinose 5-phosphate and kcat=5.9 s−1 at 37 °C. On the basis of the characterization of A. thaliana KDOPS and phylogenetic analysis, plant KDOPSs may represent a new, distinct class of KDOPSs.

Structure of mouse muskelin discoidin domain and biochemical characterization of its self-association

2014 ◽  
Vol 70 (11) ◽  
pp. 2863-2874 ◽  
Author(s):  
Kook-Han Kim ◽  
Seung Kon Hong ◽  
Kwang Yeon Hwang ◽  
Eunice EunKyeong Kim
Keyword(s):  
Crystal Structure ◽  
Cell Adhesion ◽  
Disulfide Bonds ◽  
Biochemical Characterization ◽  
Specific Interaction ◽  
Repeat Domain ◽  
Interdomain Interaction ◽  
Self Association ◽  
Cytoskeleton Dynamics

Muskelin is an intracellular kelch-repeat protein comprised of discoidin, LisH, CTLH and kelch-repeat domains. It is involved in cell adhesion and the regulation of cytoskeleton dynamics as well as being a component of a putative E3 ligase complex. Here, the first crystal structure of mouse muskelin discoidin domain (MK-DD) is reported at 1.55 Å resolution, which reveals a distorted eight-stranded β-barrel with two short α-helices at one end of the barrel. Interestingly, the N- and C-termini are not linked by the disulfide bonds found in other eukaryotic discoidin structures. A highly conserved MIND motif appears to be the determinant for MK-DD specific interaction together with the spike loops. Analysis of interdomain interaction shows that MK-DD binds the kelch-repeat domain directly and that this interaction depends on the presence of the LisH domain.

scholarly journals Identification and biochemical characterization of the fructokinase gene family in Arabidopsis thaliana

2017 ◽  
Vol 17 (1) ◽  
Author(s):  
John W. Riggs ◽  
Philip C. Cavales ◽  
Sonia M. Chapiro ◽  
Judy Callis
Keyword(s):  
Arabidopsis Thaliana ◽  
Gene Family ◽  
Biochemical Characterization

Biochemical Characterization of Cytokinin Oxidases/Dehydrogenases from Arabidopsis thaliana Expressed in Nicotiana tabacum L.

2007 ◽  
Vol 26 (3) ◽  
pp. 255-267 ◽  
Author(s):  
Petr Galuszka ◽  
Hana Popelková ◽  
Tomáš Werner ◽  
Jitka Frébortová ◽  
Hana Pospíšilová ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Nicotiana Tabacum ◽  
Biochemical Characterization ◽  
Nicotiana Tabacum L

Biochemical characterization of Arabidopsis thaliana starch branching enzyme 2.2 reveals an enzymatic positive cooperativity

Biochimie ◽  
2017 ◽  
Vol 140 ◽  
pp. 146-158 ◽  
Author(s):  
A. Wychowski ◽  
C. Bompard ◽  
F. Grimaud ◽  
G. Potocki-Véronèse ◽  
C. D'Hulst ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Biochemical Characterization ◽  
Branching Enzyme ◽  
Starch Branching Enzyme ◽  
Positive Cooperativity

scholarly journals Biochemical Characterization of Plasma Membrane H+-ATPase Activation in Guard Cell Protoplasts of Arabidopsis thaliana in Response to Blue Light

2005 ◽  
Vol 46 (6) ◽  
pp. 955-963 ◽  
Author(s):  
Kumi Ueno ◽  
Toshinori Kinoshita ◽  
Shin-ichiro Inoue ◽  
Takashi Emi ◽  
Ken-ichiro Shimazaki
Keyword(s):  
Arabidopsis Thaliana ◽  
Plasma Membrane ◽  
Blue Light ◽  
Guard Cell ◽  
Biochemical Characterization ◽  
Guard Cell Protoplasts
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