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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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The enzyme appears in viruses and cellular organisms
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
-
-
-
?
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
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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
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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
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
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
3HD4E_AGRFC
Agrobacterium fabrum (strain C58 / ATCC 33970)
342
0
36858
Swiss-Prot
T3HPD_AGRVS
Agrobacterium vitis (strain S4 / ATCC BAA-846)
342
0
36363
Swiss-Prot
T3HPD_BACC1
Bacillus cereus (strain ATCC 10987 / NRS 248)
334
0
36889
Swiss-Prot
T3HPD_BACCR
Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
334
0
36840
Swiss-Prot
T3HPD_BACHK
Bacillus thuringiensis subsp. konkukian (strain 97-27)
334
0
36841
Swiss-Prot
T3HPD_BURCH
Burkholderia cenocepacia (strain HI2424)
335
0
36329
Swiss-Prot
T3HPD_BURCM
Burkholderia ambifaria (strain ATCC BAA-244 / AMMD)
335
0
36384
Swiss-Prot
T3HPD_COLP3
Colwellia psychrerythraea (strain 34H / ATCC BAA-681)
355
0
38956
Swiss-Prot
T3HPD_LABAI
Labrenzia aggregata (strain ATCC 25650 / DSM 13394 / JCM 20685 / NBRC 16684 / NCIMB 2208 / IAM 12614)
341
0
36291
Swiss-Prot
T3HPD_PARDP
Paracoccus denitrificans (strain Pd 1222)
342
0
37450
Swiss-Prot
T3HPD_PSEAE
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
344
0
37344
Swiss-Prot
T3HPD_SHEWM
Shewanella woodyi (strain ATCC 51908 / MS32)
346
0
37985
Swiss-Prot
T3HPD_STAND
Starkeya novella (strain ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB 9113)
345
0
37028
Swiss-Prot
Y1705_SHEPA
Shewanella pealeana (strain ATCC 700345 / ANG-SQ1)
346
0
37916
Swiss-Prot
A0A2S6SR76_9PROT
340
0
38108
TrEMBL
A0A2H1I565_9MICO
337
0
35614
TrEMBL
A0A2S6SA54_9PROT
346
0
38229
TrEMBL
A0A2Z2NY64_9GAMM
345
0
37312
TrEMBL
A0A2S6UKT0_9PROT
336
0
36752
TrEMBL
H3ZMH8_THELN
Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C)
348
0
39300
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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, Azospirillum brasilense (V5YXI5)
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, Azospirillum brasilense NBRC 102289, Colwellia psychrerythraea (Q485S0), Micromonospora viridifaciens (A0A1C4WR37)
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
Azospirillum brasilense (V5YXI5), Colwellia psychrerythraea (Q485S0), Homo sapiens (Q96EM0)
brenda
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