In:
FEBS Letters, Wiley, Vol. 275, No. 1-2 ( 1990-11-26), p. 130-134
Abstract:
Construction of hybrid enzymes between the glyceraldehyde‐3‐phosphate dehydrogenases from the mesophilic Methanobacterium bryantil and the thermophilic Methanothermus fervidus by recombinant DNA techniques revealed that a short C‐terminal fragment of the Mt.fervidus enzyme contributes largely to its thermostability. This C‐terminal region appears to be homologous to the α 6 ‐helix of cubacterial and eukaryotie glyceraldehyde‐3‐phosphate dehydrogenases which is involved in the contacts between the two domains of the enzyme subunit. Site‐directed mutagenesis experiments indicate that hydrophobic interaction play an important role in these contacts.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(90)81456-X
Language:
English
Publisher:
Wiley
Publication Date:
1990
detail.hit.zdb_id:
1460391-3
SSG:
12
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