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Information on EC 1.5.1.2 - pyrroline-5-carboxylate reductase and Organism(s) Saccharolobus solfataricus and UniProt Accession Q97ZT3

for references in articles please use BRENDA:EC1.5.1.2
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IUBMB Comments
Also reduces 1-pyrroline-3-hydroxy-5-carboxylate to L-hydroxyproline.
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This record set is specific for:
Saccharolobus solfataricus
UNIPROT: Q97ZT3
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Word Map
The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The enzyme appears in selected viruses and cellular organisms
Synonyms
pycr1, proline oxidase, pyrroline-5-carboxylate reductase, p5cr, p5c reductase, 1-pyrroline-5-carboxylate reductase, delta1-pyrroline-5-carboxylate reductase, l-proline oxidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1-pyrroline-5-carboxylate reductase
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L-proline oxidase
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L-proline-NAD(P)+ 5-oxidoreductase
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L-proline:NAD(P)+ 5-oxidoreductase
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NADPH-L-DELTA'-pyrroline carboxylic acid reductase
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P5C reductase
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P5CR
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proline oxidase
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pyrroline-5-carboxylate reductase
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reductase, pyrroline-5-carboxylate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
L-proline:NAD(P)+ 5-oxidoreductase
Also reduces 1-pyrroline-3-hydroxy-5-carboxylate to L-hydroxyproline.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-17-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-pyrroline-5-carboxylate + NAD(P)H
L-proline + NAD(P)+
show the reaction diagram
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r
L-proline + NAD(P)+
1-pyrroline-5-carboxylate + NAD(P)H
show the reaction diagram
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r
L-thioproline + NAD(P)+
1-pyrroline-3-thio-5-carboxylate + NAD(P)H
show the reaction diagram
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r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
2fold preference for NADP+ with apparent KM 0.172 mM over NAD+ with apparent KM 0.3896 mM
NADP+
2fold preference for NADP+ with apparent KM 0.172 mM over NAD+ with apparent KM 0.3896 mM
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
reaction rate at pH 9.0 is nearly 3fold higher than at pH 7.0
9
reaction rate is nearly 3fold higher than at pH 7.0
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
x * 30000, SDS-PAGE. Enzyme self-associates to form large multimeric complexes. The most stable multimeric configuration is a decamer, which can further self-associate to form higher order complexes
320000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
multimer
x * 30000, SDS-PAGE. Enzyme self-associates to form large multimeric complexes. The most stable multimeric configuration is a decamer, which can further self-associate to form higher order complexes
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
diffraction to 3.5 A resolution
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
stable for at least 30 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Meng, Z.; Liu, Z.; Lou, Z.; Gong, X.; Cao, Y.; Bartlam, M.; Zhang, K.; Rao, Z.
Purification, characterization and crystallization of pyrroline-5-carboxylate reductase from the hyperthermophilic archeon Sulfolobus Solfataricus
Protein Expr. Purif.
64
125-130
2009
Saccharolobus solfataricus (Q97ZT3), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q97ZT3), Saccharolobus solfataricus P2
Manually annotated by BRENDA team