Cysteine-191 in aspartate aminotransferases appears to be conserved due to the lack of a neutral mutation pathway to the functional equivalent, alanine-191.

doi:10.1002/(SICI)1097-0134(199602)24:2<195::AID-PROT6>3.0.CO;2-I

Article

Cysteine-191 in aspartate aminotransferases appears to be conserved due to the lack of a neutral mutation pathway to the functional equivalent, alanine-191.

Proteins - 1 Feb 1996

Gloss L M, Spencer D E, Kirsch J F

Abstract excerpt

It was previously suggested that the conserved Cys-191 of aspartate aminotransferases (AATases) is conserved, not because it is essential, but because it is frozen in the sequence, with no neutral corridor to traverse to the similar phenotype of Ala-191 (Gloss et al., Biochemistry 31:32-39, 1992)...

Topics

Alanine
Amino Acid Sequence
Aspartate Aminotransferases
Conserved Sequence
Cysteine
Escherichia coli
Models, Chemical
Models, Molecular
Mutagenesis, Site-Directed
Mutation
Protein Denaturation
Structure-Activity Relationship
Urea

Cysteine-191 in aspartate aminotransferases appears to be conserved due to the lack of a neutral mutation pathway to the functional equivalent, alanine-191.

Abstract excerpt

Topics

Discuss the evidence