Stereochemistry of phosphoryl group transfer using a chiral [16O, 17O, 18O] stereochemical course of alkaline phosphatase

Nature ◽  
1978 ◽  
Vol 275 (5680) ◽  
pp. 564-565 ◽  
Author(s):  
STEPHEN R. JONES ◽  
L. ALLEN KINDMAN ◽  
JEREMY R. KNOWLES
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphoryl Group ◽  
Group Transfer

scholarly journals Routes of phosphoryl group transfer during signal transmission and signal decay in the dimeric sensor histidine kinase ArcB

2018 ◽  
Vol 293 (34) ◽  
pp. 13214-13223 ◽  
Author(s):  
Juan L. Teran-Melo ◽  
Gabriela R. Peña-Sandoval ◽  
Hortencia Silva-Jimenez ◽  
Claudia Rodriguez ◽  
Adrián F. Alvarez ◽  
...  
Keyword(s):  
Histidine Kinase ◽  
Signal Transmission ◽  
Phosphoryl Group ◽  
Sensor Histidine Kinase ◽  
Group Transfer ◽  
Signal Decay

Mechanism of Phosphoryl Group Transfer

2003 ◽  
Vol 986 (1) ◽  
pp. 275-277 ◽  
Author(s):  
L. D. FALLER ◽  
A. K. NAGY ◽  
D. J. KANE ◽  
R. A. FARLEY
Keyword(s):  
Phosphoryl Group ◽  
Group Transfer

scholarly journals High catalytic rate of the cold-active Vibrio alkaline phosphatase depends on a hydrogen bonding network involving a large interface loop

2020 ◽  
Author(s):  
Jens Guðmundur Hjörleifsson ◽  
Ronny Helland ◽  
Manuela Magnúsdóttir ◽  
Bjarni Ásgeirsson
Keyword(s):  
Alkaline Phosphatase ◽  
Temperature Stability ◽  
Catalytic Efficiency ◽  
Phosphoryl Group ◽  
Vibrio Splendidus ◽  
Large Loop ◽  
Dynamic Mobility ◽  
Catalytic Rate ◽  
Surface Loops

AbstractThe role of surface loops in mediating communication through residue networks is still a relatively poorly understood part of cold-adaptation of enzymes, especially in terms of their quaternary interactions. Alkaline phosphatase (AP) from the psychrophilic marine bacterium Vibrio splendidus (VAP) is characterized by an analogous large surface loop in each monomer, referred to as the large-loop, that hovers over the active site of the other monomer. It presumably has a role in VAP high catalytic efficiency that accompanies extremely low thermal stability. We designed several different mutagenic variants of VAP with the aim of removing inter-subunit interactions at the dimer interface. Breaking the inter-subunit contacts from one residue in particular (Arg336) caused diminished temperature stability of the catalytically potent conformation and a drop in catalytic rate by a half. The relative B-factors of the R336L crystal structure, compared to the wild-type, confirmed increased surface flexibility in a loop on the opposite monomer, but not in the large-loop. Contrary to expectations, the observed reduction in stability with an expected increase in dynamic mobility resulted in reduced catalytic rate. This contradicts common theories explaining high catalytic rates of enzyme from cold-adapted organisms as being due to reduced internal cohesion bringing increased dynamic flexibility to catalytic groups. The large-loop increases the area of the interface between the subunits through its contacts and may facilitate an alternating structural cycle demanded by a half-of-sites reaction mechanism through stronger ties, as the dimer oscillates between high affinity (active) or low phosphoryl-group affinity (inactive).

Biomimetic study of intramolecular phosphoryl group transfer in thioureas under acid/base and stereoelectronic control

1984 ◽  
Vol 106 (24) ◽  
pp. 7523-7529 ◽  
Author(s):  
C. Blonski ◽  
M. B. Gasc ◽  
A. F. Hegarty ◽  
A. Klaebe ◽  
J. J. Perie
Keyword(s):  
Phosphoryl Group ◽  
Acid Base ◽  
Group Transfer ◽  
Stereoelectronic Control
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