Abstract:
:Replacement of tryptophan 392 located in the active site cavity of pyruvate decarboxylase (PDC; EC 4.1.1.1) from Zymomonas mobilis by methionine or glutamine yields enzymes with smaller catalytic constants of 8.5 s(-1) and 3.6 s(-1) at 4 degrees C, compared to that of the wild-type enzyme (17 s(-1)). The rate constants of the H/D exchange at the C2 of the coenzyme thiamine diphosphate have been determined to be 130 s(-1) for the wild-type enzyme, 56 s(-1) for the methionine and 30 s(-1) for the glutamine mutant, respectively. A group with a pKa of about 5 has been identified to be essential for C2 deprotonation of the enzyme-bound thiamine diphosphate from the pH dependence of the H/D exchange.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Tittmann K,Mesch K,Pohl M,Hübner Gdoi
10.1016/s0014-5793(98)01594-4subject
Has Abstractpub_date
1998-12-28 00:00:00pages
404-6issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(98)01594-4journal_volume
441pub_type
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