Dinuclear Copper(II) Complexes with {Cu2(μ-hydroxo)bis(μ-carboxylato)}+Cores and Their Reactions with Sugar Phosphate Esters:  A Substrate Binding Model of Fructose-1,6-bisphosphatase

2006 ◽  
Vol 45 (7) ◽  
pp. 2925-2941 ◽  
Author(s):  
Merii Kato ◽  
Tomoaki Tanase ◽  
Masahiro Mikuriya
Keyword(s):  
Substrate Binding ◽  
Phosphate Esters ◽  
Sugar Phosphate ◽  
Binding Model ◽  
Dinuclear Copper ◽  
Fructose 1,6 Bisphosphatase

Substrate-Binding Isotherms of Spinach Chloroplastic Fructose-1,6-bisphosphatase and the Photoregulation of the Calvin Cycle

1981 ◽  
Vol 113 (3) ◽  
pp. 513-520 ◽  
Author(s):  
Jean-Claude MEUNIER ◽  
Jean BUC ◽  
Jean-Michel SOULIE ◽  
Jacques PRADEL ◽  
Jacques RICARD
Keyword(s):  
Substrate Binding ◽  
Calvin Cycle ◽  
Binding Isotherms ◽  
Fructose 1,6 Bisphosphatase

scholarly journals Structural Flexibility of Peripheral Loops and Extended C-Term Domain of Short Length Substrate Binding Protein from Rhodothermus marinus

2019 ◽  
Author(s):  
Ji-Eun Bae ◽  
In Jung Kim ◽  
Yongbin Xu ◽  
Ki Hyun Nam
Keyword(s):  
Substrate Binding ◽  
Peripheral Region ◽  
Short Length ◽  
Structural Flexibility ◽  
Rhodothermus Marinus ◽  
Binding Model ◽  
Recognition Mechanism ◽  
Comparative Structure ◽  
High Level ◽  
Electron Density Map

Substrate binding proteins (SBP) bind to specific ligands in the periplasmic region and bind to membrane proteins to participate in transport or signal transduction. Typical SBPs consist of two α/β domains and recognize the substrate by hinge motion between two domains. Conversely, short length Rhodothermus marinus SBP (named as RmSBP) exists around the methyl-accepting chemotaxis protein. We previously determined the crystal structure of RmSBP consisting of a single α/β domain, but the substrate recognition mechanism is still unclear. To better understand the short length RmSBP, we performed comparative structure analysis, computational substrate docking, and X-ray crystallographic study. RmSBP shares a high level of similarity in α/β domain with other SBP proteins, but it has a distinct topology in the C-term region. The substrate binding model suggested that conformational change in the peripheral region of RmSBP was required to recognize the substrate. We determined the crystal structures of RmSBP at pH 5.5, 6.0, and 7.5. RmSBP showed structural flexibility of the β1-α2 loop, β5-β6 loop, and extended C-term domain based on the electron density map and temperature B-factor analysis. These results provide information that will further the understanding of the function of the short length SBP.

scholarly journals Studies on the synthesis of lactose by the mammary gland. 2. The sugar-phosphate esters of milk

1952 ◽  
Vol 52 (4) ◽  
pp. 606-611 ◽  
Author(s):  
Mary G. McGeown ◽  
F. H. Malpress
Keyword(s):  
Mammary Gland ◽  
Phosphate Esters ◽  
Sugar Phosphate

Trinuclear Zn(II) and Cu(II) Homo and Heterotrimetallic Complexes Involvingd-Glucopyranosyl and Biscarboxylate Bridging Ligands. A Substrate Binding Model of Xylose Isomerases

2001 ◽  
Vol 40 (16) ◽  
pp. 3943-3953 ◽  
Author(s):  
Tomoaki Tanase ◽  
Hiromi Inukai ◽  
Tomoko Onaka ◽  
Merii Kato ◽  
Shigenobu Yano ◽  
...  
Keyword(s):  
Substrate Binding ◽  
Binding Model ◽  
Bridging Ligands

Defining a Substrate-Binding Model of a Polysialyltransferase

ChemBioChem ◽  
2013 ◽  
Vol 14 (15) ◽  
pp. 1949-1953 ◽  
Author(s):  
Friedrich Freiberger ◽  
Raphael Böhm ◽  
David Schwarzer ◽  
Rita Gerardy-Schahn ◽  
Thomas Haselhorst ◽  
...  
Keyword(s):  
Substrate Binding ◽  
Binding Model

scholarly journals Preparative-scale enzymic synthesis of d-[14C]ribulose 1,5-bisphosphate

1978 ◽  
Vol 175 (3) ◽  
pp. 909-912 ◽  
Author(s):  
G D Kuehn ◽  
T C Hsu
Keyword(s):  
Specific Radioactivity ◽  
Phosphate Esters ◽  
Sugar Phosphate ◽  
Preparative Scale ◽  
Enzymic Synthesis ◽  
Phosphogluconate Dehydrogenase ◽  
Scale Method ◽  
Coupled Reactions ◽  
Glucose 6 Phosphate Dehydrogenase

A procedure is described to prepare uniformly labelled D-[14C]ribulose 1,5-bisphosphate enzymically from uniformly labelled D-[14C]glucose through the coupled reactions catalysed by hexokinase (EC 2.7.1.1), glucose 6-phosphate dehydrogenase (EC 1.1.1.49), 6-phosphogluconate dehydrogenase (EC 1.1.1.44) and 5-phosphoribulokinase (EC 2.7.1.19). All reagents utilized in the method are commercially available. The procedure is a reliable preparative-scale method for synthesizing the dibarium salt of D-[14C]ribulose 1,5-biphosphate with a specific radioactivity up to 7 mCi/mmol and a purity near 90%. The final product was free of other 14C-labelled sugars, sugar phosphate esters, Pi and nucleotides.

scholarly journals Cover Picture: Defining a Substrate-Binding Model of a Polysialyltransferase (ChemBioChem 15/2013)

ChemBioChem ◽  
2013 ◽  
Vol 14 (15) ◽  
pp. 1909-1909
Author(s):  
Friedrich Freiberger ◽  
Raphael Böhm ◽  
David Schwarzer ◽  
Rita Gerardy-Schahn ◽  
Thomas Haselhorst ◽  
...  
Keyword(s):  
Substrate Binding ◽  
Binding Model
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