Structural relationship between the enzymatic and streptococcal binding sites of human salivary alpha-amylase.
Structural relationship between the enzymatic and streptococcal binding sites of human salivary alpha-amylase.
复制标题
人唾液α-淀粉酶的酶促和链球菌结合位点之间的结构关系。
DOI:
10.1016/s0006-291x(05)80900-3
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发表时间:
1990
影响因子:
3.1
通讯作者:
Levine,MJ
中科院分区:
文献类型:
--
作者:
Scannapieco,FA;Bhandary,K;Ramasubbu,N;Levine,MJ
Previous studies have demonstrated that human salivary α-amylase specifically binds to the oral bacteriumStreptococcus gordonii. This interaction is inhibited by substrates such as starch and maltotriose suggesting that bacterial binding may involve the enzymatic site of amylase. Experiments were performed to determine if amylase bound to the bacterial surface possessed enzymatic activity. It was found that over one-half of the bound amylase was enzymatically active. In addition, bacterial-bound amylase hydrolyzed starch to glucose which was then metabolized to lactic acid by the bacteria. In further studies, the role of amylase's histidine residues in streptococcal binding and enzymatic function was assessed after their selective modification with diethyl pyrocarbonate. DEP-modified amylase showed a marked reduction in both enzymatic and streptococcal binding activities. These effects were diminished when DEP modification occurred in the presence of maltotriose. DEP-modified amylase had a significantly altered secondary structure when compared with native enzyme or amylase modified in the presence of maltotriose. Collectively, these results suggest that human salivary α-amylase may possess multiple sites for bacterial binding and enzymatic activity which share structural similarities.
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DOI:
--
发表时间:
1989
期刊:
影响因子:
--
作者:
K. Ishikawa;H. Hirata
通讯作者:
H. Hirata
DOI:
10.1111/j.1600-0714.1973.tb01675.x
发表时间:
1973
期刊:
Journal of oral pathology
影响因子:
--
作者:
Dag Orstavik;Frederick W. Kraus
通讯作者:
Frederick W. Kraus
影响因子:
2.1
作者:
C.W.I. Douglas;A. Pease;R. Whiley
通讯作者:
R. Whiley
影响因子:
2.9
作者:
T. Rogers;R. Gold;R. Feeney
通讯作者:
R. Feeney
影响因子:
4.8
作者:
A. Loyter;M. Schramm
通讯作者:
M. Schramm