Lysine 87 in the beta subunit of tryptophan synthase that forms an internal aldimine with pyridoxal phosphate serves critical roles in transimination, catalysis, and product release.-Reference-Cited by-同舟云学术

Lysine 87 in the beta subunit of tryptophan synthase that forms an internal aldimine with pyridoxal phosphate serves critical roles in transimination, catalysis, and product release.

Published:1993-04 Issue:12 Volume:268 Page:8727-8734
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Lu Z.,Nagata S.,McPhie P.,Miles E.W.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference65 articles.

1. Carbamylation of aspartate transaminase and the pK value of the active site lysyl residue.

2. Site-directed mutagenesis of aspartate aminotransferase from E. coli

3. Substitution of an arginyl residue for the active site lysyl residue (Lys258) of aspartate aminotransferase

4. Site-specific methylation of a strategic lysyl residue in aspartate aminotransferase.

5. Direct Brønsted Analysis of the Restoration of Activity to a Mutant Enzyme by Exogenous Amines

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