Abstract:
:The NAD+-requiring enzymes of glycoside hydrolase family 4 (GHF4) contain a region with a conserved Gly-XXX-Gly-Ser (GXGS) motif near their N-termini that is reminiscent of the fingerprint region of the Rossmann fold, a conserved structural motif of classical nicotinamide nucleotide-binding proteins. The function of this putative NAD+-binding motif in the alpha-glucosidase AglA of Thermotoga maritima was probed by directed mutagenesis. The K(d) for NAD+ of the AglA mutants G10A, G12A and S13A was increased by about 300-, 5-, and 9-fold, respectively, while their K(m) for p-nitrophenyl-alpha-glucopyranoside was not seriously affected. The results indicate that the GXGS motif is indeed important for NAD+ binding by the glycosidases of GHF4.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Raasch C,Armbrecht M,Streit W,Höcker B,Sträter N,Liebl Wdoi
10.1016/s0014-5793(02)02641-8keywords:
subject
Has Abstractpub_date
2002-04-24 00:00:00pages
267-71issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579302026418journal_volume
517pub_type
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