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Information on EC 4.2.1.77 - trans-L-3-hydroxyproline dehydratase
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4.2.1.77 trans-L-3-hydroxyproline dehydrataseIUBMB Comments
Highly specific.
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Word Map
- 4.2.1.77
- trans-3-hydroxy-l-proline
- collagen
- litoralis
-
thermococcus
- analysis
- brasilense
-
azospirillum
- hydroxylase
- d-proline
- reductases
- d-lysine
- hydroxyprolines
-
prolyl
- archaeon
- l-hydroxyproline
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
AbHypG, AbLhpH, bifunctional T3LHyp dehydratase/2-epimerase, CpHypG, CpLhpH, HsLhpH, LhpH, MvHypA2, T3LHyp dehydratase, T3LHypD, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AbHypG
T3LHyp dehydratase
T3LHypD
TlLhpH
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
trans-3-hydroxy-L-proline = 1-pyrroline 2-carboxylate + H2O
highly specific, 2,3-dehydroproline is an intermediate
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
trans-L-3-hydroxyproline hydro-lyase (Delta1-pyrroline-2-carboxylate-forming)
Highly specific.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
trans-3-hydroxy-L-proline
1-pyrroline 2-carboxylate + H2O
-
-
-
?
trans-3-hydroxy-L-proline
1-pyrroline 2-carboxylate + H2O
-
-
-
-
?
trans-3-hydroxy-L-proline
1-pyrroline 2-carboxylate + H2O
-
-
-
?
trans-3-hydroxy-L-proline
1-pyrroline 2-carboxylate + H2O
-
-
-
?
trans-3-hydroxy-L-proline
1-pyrroline 2-carboxylate + H2O
-
-
-
?
trans-3-hydroxy-L-proline
1-pyrroline 2-carboxylate + H2O
the enzyme is involved in the trans-3-hydroxy-L-proline metabolism
-
-
?
trans-3-hydroxy-L-proline
1-pyrroline 2-carboxylate + H2O
-
-
-
?
trans-3-hydroxy-L-proline
1-pyrroline 2-carboxylate + H2O
the enzyme is involved in the trans-3-hydroxy-L-proline metabolism
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
trans-3-hydroxy-L-proline
1-pyrroline 2-carboxylate + H2O
-
-
-
?
trans-3-hydroxy-L-proline
1-pyrroline 2-carboxylate + H2O
-
-
-
-
?
trans-3-hydroxy-L-proline
1-pyrroline 2-carboxylate + H2O
-
-
-
?
trans-3-hydroxy-L-proline
1-pyrroline 2-carboxylate + H2O
-
-
-
?
trans-3-hydroxy-L-proline
1-pyrroline 2-carboxylate + H2O
the enzyme is involved in the trans-3-hydroxy-L-proline metabolism
-
-
?
trans-3-hydroxy-L-proline
1-pyrroline 2-carboxylate + H2O
the enzyme is involved in the trans-3-hydroxy-L-proline metabolism
-
-
?
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dehydration
Characterization of a Novel cis-3-Hydroxy-l-Proline Dehydratase and a trans-3-Hydroxy-l-Proline Dehydratase from Bacteria.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00291
trans-3-hydroxy-L-proline
pH 8.0, 30°C, wild-type enzyme
0.0472
trans-3-hydroxy-L-proline
pH 8.0, 30°C, mutant enzyme C261T
2.79
trans-3-hydroxy-L-proline
pH 8.0, 30°C, wild-type enzyme
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.43
trans-3-hydroxy-L-proline
pH 8.0, 30°C, mutant enzyme C261T
3.4
trans-3-hydroxy-L-proline
pH 8.0, 30°C, wild-type enzyme
22.17
trans-3-hydroxy-L-proline
pH 8.0, 30°C, wild-type enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.052
trans-3-hydroxy-L-proline
pH 8.0, 30°C, mutant enzyme C261T
7.95
trans-3-hydroxy-L-proline
pH 8.0, 30°C, wild-type enzyme
42.7
trans-3-hydroxy-L-proline
pH 8.0, 30°C, wild-type enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.877
substrate: trans-3-hydroxy-L-proline, pH 8.0, 30°C, mutant enzyme C261T
17.6
substrate: trans-3-hydroxy-L-proline, pH 8.0, 30°C, wild-type enzyme
25.4
26.1
25.4
substrate: trans-3-hydroxy-L-proline, pH 8.0, 30°C, wild-type enzyme
26.1
-
substrate: trans-3-hydroxy-L-proline, pH 8.0, 30°C, wild-type enzyme
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
the enzyme is involved in the trans-3-hydroxy-L-proline metabolism
metabolism
the enzyme is involved in the trans-3-hydroxy-L-proline pathway. The trans-3-hydroxy-L-proline pathway is not linked to trans-4-hydroxy-L-proline and L-proline metabolism
metabolism
-
the enzyme is involved in the trans-3-hydroxy-L-proline metabolism
-
Show AA Sequence and Transmembrane Helices (743 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C261T
C261T
-
the kcat/Km value is 826fold lower than that of the wild-type enzyme, and this is mainly attributed to a 162fold increase in Km
C261T
-
the kcat/Km value is 826fold lower than that of the wild-type enzyme, and this is mainly attributed to a 162fold increase in Km
-
C261T
the kcat/Km value is 826fold lower than that of the wild-type enzyme, and this is mainly attributed to a 162fold increase in Km
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21(DE3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
induced by trans-3-hydroxy-L-proline (and D-proline and D-lysine) but not trans-4-hydroxy-L-proline
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
analysis
estimation of the content of L-hydroxyprolines using coupling systems with metabolic enzymes of the trans-4-hydroxy-L-proline pathway (hydroxyproline 2-epimerase (HypE) and cis-4-hydroxy-D-proline dehydrogenase (HypDH)) and the trans-3-hydroxy-L-proline pathway (trans-3-hydroxy-L-proline dehydratase (T3LHypD) and DELTA1-pyrroline-2-carboxylate reductase (Pyr2CR)) from microorganisms. A functional expression system of recombinant HypDH with a heterooligomeric structure is constructed in Escherichia coli cells. Enzymological characterization reveals that the beta-subunit acts as a catalytic subunit, and also that assembly with other subunit(s) improves the kinetics for cis-4-hydroxy-D-proline and thermostability. By using a spectrophotometric assay with different wavelengths, the contents of trans-4-hydroxy-L-proline and trans-3-hydroxy-L-proline are successfully estimated within the ranges of 0.004-1 mM and 0.05-1 mM, respectively, and are consistent with the contents determined by HPLC. This enzymatic method is used to measure the content of trans-4-hydroxy-L-proline in the acid-hydrolysate of collagen, and blood plasma
analysis
estimation of the content of L-hydroxyprolines using coupling systems with metabolic enzymes of the trans-4-hydroxy-L-proline pathway (hydroxyproline 2-epimerase (HypE) and cis-4-hydroxy-D-proline dehydrogenase (HypDH)) and the trans-3-hydroxy-L-proline pathway (trans-3-hydroxy-L-proline dehydratase (T3LHypD) and DELTA1-pyrroline-2-carboxylate reductase (Pyr2CR)) from microorganisms. A functional expression system of recombinant HypDH with a heterooligomeric structure is constructed in Escherichia coli cells. Enzymological characterization reveals that the beta-subunit acts as a catalytic subunit, and also that assembly with other subunit(s) improves the kinetics for cis-4-hydroxy-D-proline and thermostability. By using a spectrophotometric assay with different wavelengths, the contents of trans-4-hydroxy-L-proline and trans-3-hydroxy-L-proline are successfully estimated within the ranges of 0.004-1 mM and 0.05-1 mM, respectively, and are consistent with the contents determined by HPLC. This enzymatic method is used to measure the content of trans-4-hydroxy-L-proline in the acid-hydrolysate of collagen, and blood plasma
analysis
estimation of the content of L-hydroxyprolines using coupling systems with metabolic enzymes of the trans-4-hydroxy-L-proline pathway (hydroxyproline 2-epimerase (HypE) and cis-4-hydroxy-D-proline dehydrogenase (HypDH)) and the trans-3-hydroxy-L-proline pathway (trans-3-hydroxy-L-proline dehydratase (T3LHypD) and DELTA1-pyrroline-2-carboxylate reductase (Pyr2CR)) from microorganisms. A functional expression system of recombinant HypDH with a heterooligomeric structure is constructed in Escherichia coli cells. Enzymological characterization reveals that the beta-subunit acts as a catalytic subunit, and also that assembly with other subunit(s) improves the kinetics for cis-4-hydroxy-D-proline and thermostability. By using a spectrophotometric assay with different wavelengths, the contents of trans-4-hydroxy-L-proline and trans-3-hydroxy-L-proline are successfully estimated within the ranges of 0.004-1 mM and 0.05-1 mM, respectively, and are consistent with the contents determined by HPLC. This enzymatic method is used to measure the content of trans-4-hydroxy-L-proline in the acid-hydrolysate of collagen, and blood plasma
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ramaswamy, S.G.
Conversion of 3-hydroxyproline to proline in the rat rquires reduced pyridine nucleotides
Fed. Proc.
42
2232
1983
Rattus norvegicus
-
brenda
Watanabe, S.; Tozawa, Y.; Watanabe, Y.
Ornithine cyclodeaminase/mu-crystallin homolog from the hyperthermophilic archaeon Thermococcus litoralis functions as a novel DELTA(1)-pyrroline-2-carboxylate reductase involved in putative trans-3-hydroxy-L-proline metabolism
FEBS Open Bio
4
617-626
2014
Thermococcus litoralis (H3ZMH8), Thermococcus litoralis, Thermococcus litoralis DSM 5473 (H3ZMH8), Thermococcus litoralis DSM 5473
brenda
Watanabe, S.; Tanimoto, Y.; Yamauchi, S.; Tozawa, Y.; Sawayama, S.; Watanabe, Y.
Identification and characterization of trans-3-hydroxy-l-proline dehydratase and DELTA1-pyrroline-2-carboxylate reductase involved in trans-3-hydroxy-l-proline metabolism of bacteria
FEBS Open Bio
4
240-250
2014
Azospirillum brasilense (V5YXI5), Azospirillum brasilense
brenda
Watanabe, S.; Fukumori, F.; Miyazaki, M.; Tagami, S.; Watanabe, Y.
Characterization of a novel cis-3-hydroxy-L-proline dehydratase and a trans-3-hydroxy-L-proline dehydratase from Bacteria
J. Bacteriol.
199
e00255-17
2017
Azospirillum brasilense, Micromonospora viridifaciens (A0A1C4WR37), Colwellia psychrerythraea (Q485S0), Azospirillum brasilense NBRC 102289
brenda
Watanabe, S.; Hiraoka, Y.; Endo, S.; Tanimoto, Y.; Tozawa, Y.; Watanabe, Y.
An enzymatic method to estimate the content of L-hydroxyproline
J. Biotechnol.
199
9-16
2015
Colwellia psychrerythraea (Q485S0), Homo sapiens (Q96EM0), Azospirillum brasilense (V5YXI5)
brenda
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