Unknown

Dataset Information

0

Direct Enzymatic Synthesis of a Deep-Blue Fluorescent Noncanonical Amino Acid from Azulene and Serine.


ABSTRACT: We report a simple, one-step enzymatic synthesis of the blue fluorescent noncanonical amino acid ?-(1-azulenyl)-l-alanine (AzAla). By using an engineered tryptophan synthase ?-subunit (TrpB), stereochemically pure AzAla can be synthesized at scale starting from commercially available azulene and l-serine. Mutation of a universally conserved catalytic glutamate in the active site to glycine has only a modest effect on native activity with indole but abolishes activity on azulene, suggesting that this glutamate activates azulene for nucleophilic attack by stabilization of the aromatic ion.

SUBMITTER: Watkins EJ 

PROVIDER: S-EPMC6980211 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature

altmetric image

Publications

Direct Enzymatic Synthesis of a Deep-Blue Fluorescent Noncanonical Amino Acid from Azulene and Serine.

Watkins Ella J EJ   Almhjell Patrick J PJ   Arnold Frances H FH  

Chembiochem : a European journal of chemical biology 20191118 1-2


We report a simple, one-step enzymatic synthesis of the blue fluorescent noncanonical amino acid β-(1-azulenyl)-l-alanine (AzAla). By using an engineered tryptophan synthase β-subunit (TrpB), stereochemically pure AzAla can be synthesized at scale starting from commercially available azulene and l-serine. Mutation of a universally conserved catalytic glutamate in the active site to glycine has only a modest effect on native activity with indole but abolishes activity on azulene, suggesting that  ...[more]

Similar Datasets

| S-EPMC7709965 | biostudies-literature
| S-EPMC6434697 | biostudies-literature
| S-EPMC5468623 | biostudies-literature
| S-EPMC6508085 | biostudies-literature
2023-10-06 | GSE214494 | GEO
| S-EPMC2517582 | biostudies-literature
2024-09-30 | GSE271876 | GEO
| S-EPMC8104435 | biostudies-literature
| S-EPMC4490519 | biostudies-literature
| S-EPMC8296014 | biostudies-literature