1994
DOI: 10.1271/bbb.58.807
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Kinetics of Thermostable Alanine Racemase ofBacillus stearothermophilus

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Cited by 11 publications
(10 citation statements)
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“…Sawada et al (1) have proposed on the basis of kinetic evidence that the reaction catalyzed by BSAR proceeds through a two-base mechanism. Shaw et al (2) have postulated on the basis of x-ray crystallographic studies that Lys 39 and Tyr 265 of BSAR serve as the bases to abstract ␣-hydrogen from the alanyl-PLP aldimine and to protonate the carbanion intermediate to give the alanyl-PLP aldimine.…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…Sawada et al (1) have proposed on the basis of kinetic evidence that the reaction catalyzed by BSAR proceeds through a two-base mechanism. Shaw et al (2) have postulated on the basis of x-ray crystallographic studies that Lys 39 and Tyr 265 of BSAR serve as the bases to abstract ␣-hydrogen from the alanyl-PLP aldimine and to protonate the carbanion intermediate to give the alanyl-PLP aldimine.…”
Section: Resultsmentioning
confidence: 99%
“…Alanine racemase (EC 5.1.1.1) is a pyridoxal 5Ј-phosphate (PLP) 1 enzyme that occurs widely in bacteria and plays a central role in the metabolism of D-alanine, an essential component of the peptidoglycans in bacterial cell walls. The generally accepted mechanism of alanine racemase reaction proceeds through the steps shown in Scheme I. PLP bound with the active-site lysyl residue (A) reacts with a substrate to form an external Schiff base (B) through transaldimination.…”
mentioning
confidence: 99%
“…The mechanism of alanine racemase follows a twobase mechanism [65,66] (Scheme 10). In the absence of substrate, PLP is ×chemically stored× in the active site via binding though an internal Schiff-base (aldimine) formation involving the e-NH 2 -group of Lys39.…”
Section: The Enzymementioning
confidence: 99%
“…They suggested that Tyr-265 and Lys-39, the PLP binding lysine, serve as the bases. Sawada et al have presented kinetic evidence to show that the alanine racemase reaction follows a two-base mechanism (40). The stereospecificity for the hydrogen transfer reflects the structure of the active site of pyridoxal enzymes, especially the topographical relationship between the catalytic base for the hydrogen transfer and the bound coenzyme.…”
Section: Stereospecificity Of Amino Acid Racemases For Hydrogen Abstrmentioning
confidence: 99%