Structural aspects of the allosteric inhibition of fructose-1,6-bisphosphatase by AMP: the binding of both the substrate analogue 2,5-anhydro-D-glucitol 1,6-bisphosphate and catalytic metal ions monitored by X-ray crystallography

Structural aspects of the allosteric inhibition of fructose-1,6-bisphosphatase by AMP: the binding of both the substrate analogue 2,5-anhydro-D-glucitol 1,6-bisphosphate and catalytic metal ions monitored by X-ray crystallography

Item
http://www.wikidata.org/entity/Q27729929
Crystallographic evidence for the action of potassium, thallium, and lithium ions on fructose-1,6-bisphosphataseThe N-terminal segment of recombinant porcine fructose-1,6-bisphosphatase participates in the allosteric regulation of catalysis.Evidence for an active T-state pig kidney fructose 1,6-bisphosphatase: interface residue Lys-42 is important for allosteric inhibition and AMP cooperativity.Crystal structures of the active site mutant (Arg-243-->Ala) in the T and R allosteric states of pig kidney fructose-1,6-bisphosphatase expressed in Escherichia coli.Directed mutations in the poorly defined region of porcine liver fructose-1,6-bisphosphatase significantly affect catalysis and the mechanism of AMP inhibition.Different sensitivities of mutants and chimeric forms of human muscle and liver fructose-1,6-bisphosphatases towards AMP.Kinetic analysis of product release and metal ions in a metallonuclease.Site-directed mutagenesis of residues at subunit interfaces of porcine fructose-1,6-bisphosphatase.Minimum MD simulation length required to achieve reliable results in free energy perturbation calculations: case study of relative binding free energies of fructose-1,6-bisphosphatase inhibitors.Regulation of the Calvin-Benson-Bassham cycle in the enigmatic diatoms: biochemical and evolutionary variations on an original theme.Spontaneous subunit exchange in porcine liver fructose-1,6-bisphosphatase.Binding of AMP to two of the four subunits of pig kidney fructose-1,6-bisphosphatase induces the allosteric transition.Bisubstrate inhibitors for the enzyme catechol-O-methyltransferase (COMT): influence of inhibitor preorganisation and linker length between the two substrate moieties on binding affinity.
P2860

Structural aspects of the allosteric inhibition of fructose-1,6-bisphosphatase by AMP: the binding of both the substrate analogue 2,5-anhydro-D-glucitol 1,6-bisphosphate and catalytic metal ions monitored by X-ray crystallography

Item
http://www.wikidata.org/entity/Q27729929
description
1995 nî lūn-bûn
@nan
1995 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Structural aspects of the allo ...... tored by X-ray crystallography
@ast
Structural aspects of the allo ...... tored by X-ray crystallography
@en
Structural aspects of the allo ...... tored by X-ray crystallography
@nl
type
label
Structural aspects of the allo ...... tored by X-ray crystallography
@ast
Structural aspects of the allo ...... tored by X-ray crystallography
@en
Structural aspects of the allo ...... tored by X-ray crystallography
@nl
prefLabel
Structural aspects of the allo ...... tored by X-ray crystallography
@ast
Structural aspects of the allo ...... tored by X-ray crystallography
@en
Structural aspects of the allo ...... tored by X-ray crystallography
@nl
P1433
P1476
P2093
P304
P31
P356
P407
P433
P478
P50
P577
P698
P921
P356
P1433
P1476
Structural aspects of the allo ...... tored by X-ray crystallography
@en
P2093
P304
P31
P356
P407
P433
P478
P50
P577
P698
P921