3.5.2.9: 5-oxoprolinase (ATP-hydrolysing)
This is an abbreviated version!
For detailed information about 5-oxoprolinase (ATP-hydrolysing), go to the full flat file.
Word Map on EC 3.5.2.9
-
3.5.2.9
-
5-oxoproline
-
gamma-glutamyl
-
5-oxoprolinuria
-
l-2-oxothiazolidine-4-carboxylate
-
medicine
-
cyclotransferase
-
decyclization
-
gamma-glutamyl-cysteine
-
atp-hydrolyzing
-
meister
- 3.5.2.9
- 5-oxoproline
-
gamma-glutamyl
-
5-oxoprolinuria
- l-2-oxothiazolidine-4-carboxylate
- medicine
-
cyclotransferase
-
decyclization
-
gamma-glutamyl-cysteine
-
atp-hydrolyzing
-
meister
Reaction
Synonyms
5-OPase, 5-oxo-L-prolinase, 5-oxoprolinase, 5OPase, ATP-dependent 5-oxoprolinase, FgOXP1, FgOXP2, FGSG_04902, FGSG_10203, L-pyroglutamate hydrolase, OPase, oplA, OPLAH, oxoprolinase, OXP1, PA4511, prokaryotic 5-oxoprolinase, PxpA, pxpA3, pxpB, pxpC, pyroglutamase, pyroglutamase (ATP-hydrolysing), pyroglutamate hydrolase, pyroglutamic hydrolase, SSO1667
ECTree
Advanced search results
Subunits
Subunits on EC 3.5.2.9 - 5-oxoprolinase (ATP-hydrolysing)
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
dimer
polymer
additional information
-
2 protein compounds, component A exhibits 5-oxo-L-proline depedent ATPase activity, component A composed of 6 heterodimers, 6 * 51000 + 6 * 64000, SDS-PAGE, component B is a coupling protein without ATPase activity, 8 * 82000, octamer, SDS-PAGE
polymer
-
component A 1 * 65500 + 1 * 50000, component B 1 * 80000, SDS-PAGE
additional information
structural bioinformatics analysis of four putative PxpA structures reveal that PxpA adopts a non-canonical TIM barrel fold with well-characterized TIM barrel enzyme features. Structure-function relationships of 5-oxoprolinase subunit A. Four putative PxpA three-dimensional structures are determined by structural genomics initiatives
additional information
-
structural bioinformatics analysis of four putative PxpA structures reveal that PxpA adopts a non-canonical TIM barrel fold with well-characterized TIM barrel enzyme features. Structure-function relationships of 5-oxoprolinase subunit A. Four putative PxpA three-dimensional structures are determined by structural genomics initiatives
-
additional information
-
structural bioinformatics analysis of four putative PxpA structures reveal that PxpA adopts a non-canonical TIM barrel fold with well-characterized TIM barrel enzyme features. Structure-function relationships of 5-oxoprolinase subunit A. Four putative PxpA three-dimensional structures are determined by structural genomics initiatives
-
additional information
-
structural bioinformatics analysis of four putative PxpA structures reveal that PxpA adopts a non-canonical TIM barrel fold with well-characterized TIM barrel enzyme features. Structure-function relationships of 5-oxoprolinase subunit A. Four putative PxpA three-dimensional structures are determined by structural genomics initiatives
-
additional information
-
structural bioinformatics analysis of four putative PxpA structures reveal that PxpA adopts a non-canonical TIM barrel fold with well-characterized TIM barrel enzyme features. Structure-function relationships of 5-oxoprolinase subunit A. Four putative PxpA three-dimensional structures are determined by structural genomics initiatives
-
additional information
-
structural bioinformatics analysis of four putative PxpA structures reveal that PxpA adopts a non-canonical TIM barrel fold with well-characterized TIM barrel enzyme features. Structure-function relationships of 5-oxoprolinase subunit A. Four putative PxpA three-dimensional structures are determined by structural genomics initiatives
-
additional information
-
structural bioinformatics analysis of four putative PxpA structures reveal that PxpA adopts a non-canonical TIM barrel fold with well-characterized TIM barrel enzyme features. Structure-function relationships of 5-oxoprolinase subunit A. Four putative PxpA three-dimensional structures are determined by structural genomics initiatives
-
additional information
-
structural bioinformatics analysis of four putative PxpA structures reveal that PxpA adopts a non-canonical TIM barrel fold with well-characterized TIM barrel enzyme features. Structure-function relationships of 5-oxoprolinase subunit A. Four putative PxpA three-dimensional structures are determined by structural genomics initiatives
-