The E104D mutation increases the susceptibility of human triosephosphate isomerase to proteolysis. Asymmetric cleavage of the two monomers of the homodimeric enzyme
Journal Article
·
· BBA- Proteins Proteom.
- INP-Mexico
- Research Organization:
- Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
- Sponsoring Organization:
- FOREIGN
- OSTI ID:
- 1104561
- Journal Information:
- BBA- Proteins Proteom., Vol. 1834, Issue (12) ; 12, 2013
- Country of Publication:
- United States
- Language:
- ENGLISH
Similar Records
Enzyme Architecture: The Effect of Replacement and Deletion Mutations of Loop 6 on Catalysis by Triosephosphate Isomerase
Human triosephosphate isomerase deficiency resulting from mutation of Phe-240
Structural Basis of Human Triosephosphate Isomerase Deficiency: Mutation E104D is Related to Alterations of a Conserved Water Network at the Dimer Interface
Journal Article
·
Thu Jul 10 00:00:00 EDT 2014
· Biochemistry-US
·
OSTI ID:1104561
+6 more
Human triosephosphate isomerase deficiency resulting from mutation of Phe-240
Journal Article
·
Tue Jun 01 00:00:00 EDT 1993
· American Journal of Human Genetics; (United States)
·
OSTI ID:1104561
+3 more
Structural Basis of Human Triosephosphate Isomerase Deficiency: Mutation E104D is Related to Alterations of a Conserved Water Network at the Dimer Interface
Journal Article
·
Thu Jan 07 00:00:00 EST 2010
· J. Biol. Chem.
·
OSTI ID:1104561
+6 more