volume 85, issue 4, P694-708 2017
DOI: 10.1002/prot.25249
View full text
|
|
Share

Abstract: A conserved cis proline residue located in the active site of Thermotoga maritima acetyl esterase (TmAcE) from the carbohydrate esterase family 7 (CE7) has been substituted by alanine. The residue was known to play a crucial role in determining the catalytic properties of the enzyme. To elucidate the structural role of the residue, the crystal structure of the Pro228Ala variant (TmAcE ) was determined at 2.1 Å resolution. The replacement does not affect the overall secondary, tertiary, and quaternary structure…

Expand abstract

Search citation statements

Order By: Relevance

Citation Types

0
5
0

Paper Sections

0
0
0
0
0

Publication Types

0
0
0
0

Relationship

0
0

Authors

Journals