Substrate-mediated electron transfer in peptidylglycine α-hydroxylating monooxygenase
Substrate-mediated electron transfer in peptidylglycine α-hydroxylating monooxygenase
复制标题
肽基甘氨酸 α-羟基化单加氧酶中底物介导的电子转移
DOI:
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发表时间:
1999
期刊:
影响因子:
--
通讯作者:
R. Mains
中科院分区:
文献类型:
--
作者:
L. Amzel;S. Prigge;A. Kolhekar;B. Eipper;R. Mains
Peptide amidation is a ubiquitous posttranslational modification of bioactive peptides. Peptidylglycine α-hydroxylating monooxygenase (PHM; EC 1.14.17.3), the enzymne that catalyzes the first step of this reaction, is composed of two domains, each of which binds one copper atom. The coppers are held 11 Å apart on either side of a solvent-filled interdomain cleft, and the PHM reaction requires electron transfer between these sites. A plausible mechanism for electron transfer might involve interdomain motion to decrease the distance between the copper atoms. Our experiments show that PHM catalytic core (PHMcc) is enzymatically active in the crystal phase, where interdomain motion is not possible. Instead, structures of two states relevant to catalysis indicate that water, substrate and active site residues may provide an electron transfer pathway that exists only during the PHM catalytic cycle.
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DOI:
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发表时间:
1984
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Westbrook,EM;Sigler,PB
通讯作者:
Sigler,PB
DOI:
10.1073/pnas.95.16.9220
发表时间:
1998-08-04
影响因子:
11.1
作者:
Vásquez-Vivar, J;Kalyanaraman, B;Pritchard, KA
通讯作者:
Pritchard, KA
影响因子:
3.9
作者:
Kulathila,R;Consalvo,AP;Fitzpatrick,PF;Freeman,JC;Snyder,LM;Villafranca,JJ;Merkler,DJ
通讯作者:
Merkler,DJ
DOI:
10.1210/mend-1-4-290
发表时间:
1987
期刊:
Molecular endocrinology (Baltimore, Md.)
影响因子:
--
作者:
Murthy,AS;Keutmann,HT;Eipper,BA
通讯作者:
Eipper,BA