ISSN:
1573-4943
Keywords:
Pyridoxal
;
pyridoxal 5′-phosphate
;
salicylaldehyde
;
mechanism of B6-vitamin-dependent enzymes
;
acidity in organic solvents
;
tautomerism
;
protolytic equilibria
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract The enzymatic reactions involving pyridoxal 5′-phosphate (PLP) can be simulated in solutions; thus, this system forms a favorable model for understanding the requirements of the enzymatic catalysis. We have studied in methanol protonic equilibria of the imines formed between PLP or salicylaldehyde (SA) and various amino acids, using UV and NMR spectroscopy. A glass electrode and an operationalpH* scale were used to control acidity. The first protonation of the phosphate of PLP imines can be detected by UV spectroscopy withpK* at 10.8, proved by [31P]-NMR. The second protonation of phosphate (pK* at 4.8) is accompanied by increased hydrolysis of the imines. The imines of aspartate deviate from the imines of nondicarboxylic amino acids indicating that the β-carboxyl of aspartate is internally hydrogen-bonded. PLP-2-aminobutanol Schiff base does not show with [1H]-NMR atpH* 7 separate peaks for ketoenamine-enolimine tautomers even at -90°C, SA-phenylalanine shows an unidentified absorption at 350–380 nm. This was tentatively assigned a trans structure.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01024873
Permalink
