Information on EC 4.2.1.171 - cis-L-3-hydroxyproline dehydratase

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The expected taxonomic range for this enzyme is: Labrenzia aggregata

EC NUMBER
COMMENTARY hide
4.2.1.171
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RECOMMENDED NAME
GeneOntology No.
cis-L-3-hydroxyproline dehydratase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
cis-3-hydroxy-L-proline = 1-pyrroline-2-carboxylate + H2O
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine and proline metabolism
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SYSTEMATIC NAME
IUBMB Comments
cis-3-hydroxy-L-proline hydro-lyase (1-pyrroline-2-carboxylate-forming)
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
cis-3-hydroxy-L-proline
1-pyrroline-2-carboxylate + H2O
show the reaction diagram
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?
additional information
?
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the enzyme catalyzes the competing 2-epimerization to trans-3-hydroxy-D-proline (1,1-proton transfer) and dehydration to 1-pyrroline-2-carboxylate (beta-elimination), with eventual total dehydration. The reactions are initiated by abstraction of the alpha-proton of the substrate. The rate of epimerization is about 1.5fold greater than that of dehydration at substrate concentrations both below and above the value of the KM. No substrates: L-proline and stereoisomers of 3-hydroxyproline, 4-hydroxyproline and their mono- and di-N-methylated derivatives
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.1
cis-3-hydroxy-L-proline
pH 8.0, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
23
cis-3-hydroxy-L-proline
pH 8.0, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.8
cis-3-hydroxy-L-proline
pH 8.0, temperature not specified in the publication
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with Mg2+, to 2.2 A resolution
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K165A
mutation in general acid/base residue, complete loss of activity
K265A
mutation in general acid/base residue, complete loss of activity