Literature DB >> 6305412

Cryospectroscopy of intermediates in the mechanism of carboxypeptidase A.

K F Geoghegan, A Galdes, R A Martinelli, B Holmquist, D S Auld, B L Vallee.   

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Year:  1983        PMID： 6305412     DOI： 10.1021/bi00278a031

Source DB:  PubMed          Journal:  Biochemistry        ISSN： 0006-2960            Impact factor:   3.162


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  5 in total

1.  Direct observation of enzyme substrate complexes by stopped-flow fluorescence: mathematical analyses.

Authors:  R R Lobb; D S Auld
Journal:  Experientia       Date:  1984-11-15

2.  Stopped-flow cryoenzymology: detection of catalytic intermediates not observable at ambient temperatures.

Authors:  H E Van Wart; S H Lin
Journal:  Proc Natl Acad Sci U S A       Date:  1983-12       Impact factor: 11.205

3.  Crystallographic studies on apocarboxypeptidase A and the complex with glycyl-L-tyrosine.

Authors:  D C Rees; W N Lipscomb
Journal:  Proc Natl Acad Sci U S A       Date:  1983-12       Impact factor: 11.205

4.  Catalysis of carboxypeptidase A: promoted-water versus nucleophilic pathways.

Authors:  Shanshan Wu; Chunchun Zhang; Dingguo Xu; Hua Guo
Journal:  J Phys Chem B       Date:  2010-07-22       Impact factor: 2.991

5.  Cryospectrokinetic characterization of intermediates in biochemical reactions: carboxypeptidase A.

Authors:  D S Auld; A Galdes; K F Geoghegan; B Holmquist; R A Martinelli; B L Vallee
Journal:  Proc Natl Acad Sci U S A       Date:  1984-08       Impact factor: 11.205
  5 in total

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