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Information on EC 1.5.99.B2 - proline dehydrogenase (acceptor) and Organism(s) Deinococcus radiodurans and UniProt Accession Q9RW55

for references in articles please use BRENDA:EC1.5.99.B2
preliminary BRENDA-supplied EC number
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Deinococcus radiodurans
UNIPROT: Q9RW55 not found.
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The taxonomic range for the selected organisms is: Deinococcus radiodurans
The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria
Synonyms
prodh2, pro dehydrogenase, l-prodh, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
L-proline:acceptor oxidoreductase
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-proline + coenzyme Q1 + H2O
DELTA1-pyrroline-5-carboxylate + reduced coenzyme Q1
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.028 - 0.155
coenzyme Q1
50 - 384
L-proline
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.043 - 14
coenzyme Q1
0.055 - 8.7
L-proline
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme in the oxidized state complexed with the proline analogue L-tetrahydrofuroic acid and in the reduced state with the proline site vacant, sitting drop vapor diffusion method, using 0.2 M MgCl2, 25% (w/v) PEG 3350, and 0.1 mM Bis-Tris (pH 5.8), at 22°C
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E64A
the mutation decreases the catalytic efficiency 27fold
G63A
the mutation decreases the catalytic efficiency 140fold
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography and Hitrap Q column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)pLysS cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Luo, M.; Arentson, B.W.; Srivastava, D.; Becker, D.F.; Tanner, J.J.
Crystal structures and kinetics of monofunctional proline dehydrogenase provide insight into substrate recognition and conformational changes associated with flavin reduction and product release
Biochemistry
51
10099-10108
2012
Deinococcus radiodurans (Q9RW55)
Manually annotated by BRENDA team