In:
European Journal of Biochemistry, Wiley, Vol. 192, No. 3 ( 1990-09), p. 627-631
Abstract:
With increasing SDS/protein ratios, covalent phosphorylation by ATP and P i is abolished before ATP hydrolysis (P i production) ceases. We have shown that the SDS‐dependent profiles of the decline in covalent phosphorylation by either substrate are virtually identical, reflecting a common mechanism of detergent interaction, while ATP can be hydrolysed via a non‐covalent phosphointermediate. Our studies support that the transfer of both terminal P i from ATP, as well as P i to its final binding site, is a multistep reaction involving electrostatic interaction with one or more amino acid side chains, including a Lys residue.
Type of Medium:
Online Resource
ISSN:
0014-2956
,
1432-1033
DOI:
10.1111/ejb.1990.192.issue-3
DOI:
10.1111/j.1432-1033.1990.tb19269.x
Language:
English
Publisher:
Wiley
Publication Date:
1990
detail.hit.zdb_id:
1398347-7
detail.hit.zdb_id:
2172518-4
SSG:
12
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