Literature DB >> 4201665

Transition-state analogs of an aliphatic amidase.

J D Findlater, B A Orsi.   

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Year:  1973        PMID： 4201665     DOI： 10.1016/0014-5793(73)80588-5

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


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  5 in total

1.  Substitution of Glu-59 by Val in amidase from Pseudomonas aeruginosa results in a catalytically inactive enzyme.

Authors:  A Karmali; R Tata; P R Brown
Journal:  Mol Biotechnol       Date:  2000-09       Impact factor: 2.695

2.  Binding of a possible transition state analogue to the active site of carboxypeptidase A.

Authors:  D W Christianson; W N Lipscomb
Journal:  Proc Natl Acad Sci U S A       Date:  1985-10       Impact factor: 11.205

3.  Relationship between mutant amidases of Pseudomonas aeruginosa and hydroxyurea as an inhibitor.

Authors:  P R Brown; M Gregoriou; R Tata
Journal:  Mol Gen Genet       Date:  1978-10-04

4.  Crystallization, diffraction data collection and preliminary crystallographic analysis of hexagonal crystals of Pseudomonas aeruginosa amidase.

Authors:  Jorge Andrade; Amin Karmali; Maria A Carrondo; Carlos Frazão
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2007-02-23

5.  Chloroacetone as an active-site-directed inhibitor of the aliphatic amidase from Pseudomonas aeruginosa.

Authors:  M R Hollaway; P H Clarke; T Ticho
Journal:  Biochem J       Date:  1980-12-01       Impact factor: 3.857
  5 in total

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