BRENDA - Enzyme Database
show all sequences of 1.5.5.2

Proline dehydrogenase from Thermus thermophilus does not discriminate between FAD and FMN as cofactor

Huijbers, M.M.; Martinez-Julvez, M.; Westphal, A.H.; Delgado-Arciniega, E.; Medina, M.; van Berkel, W.J.; Sci. Rep. 7, 43880 (2017)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
recombinant expression of the holo form of MBP-tagged TtProDH in Escherichia coli TOP10 cells, the recombinant enzyme contains about three times more FMN than FAD. The apoenzyme is produced by riboflavin auxotrophic Escherichia coli strain BSV11 and can be successfully reconstituted with FAD or FMN. The recombinant apo-enzyme reconstituted with FAD or FMN shows equal specific activities as holo-enzyme
Thermus thermophilus
Crystallization (Commentary)
Crystallization (Commentary)
Organism
purified TtProDH mutant variant DELTAABC lacking helices alphaA, alphaB and alphaC, X-ray diffraction structure determination and analysis at 2.2 A resolution
Thermus thermophilus
Engineering
Protein Variants
Commentary
Organism
F10E/L12E
construction of a variant with a more polar N-terminus, mutant F10E/L12E, because Thermus thermophilus ProDH (TtProDH), produced through fusion with maltose-binding protein (MBP) appears to be prone to aggregation. Preparation of TtProDH mutant variant DELTAABC, which lacks helices alphaA, alphaB and alphaC, the mutant shows no electron density for an AMP moiety of the cofactor
Thermus thermophilus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
36.6
-
L-proline
recombinant apo-enzyme reconstituted with FAD, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol
Thermus thermophilus
50.1
-
L-proline
recombinant apo-enzyme reconstituted with FMN, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol
Thermus thermophilus
76.6
-
L-proline
recombinant holo-enzyme, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol
Thermus thermophilus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
L-proline + a quinone
Thermus thermophilus
the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2
(S)-1-pyrroline-5-carboxylate + a quinol
-
-
ir
L-proline + a quinone
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2
(S)-1-pyrroline-5-carboxylate + a quinol
-
-
ir
Organism
Organism
UniProt
Commentary
Textmining
Thermus thermophilus
Q72IB8
-
-
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Q72IB8
-
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.84
-
purified recombinant apo-enzyme, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol
Thermus thermophilus
4.74
-
purified recombinant holo-enzyme, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol
Thermus thermophilus
4.83
-
purified recombinant apo-enzyme reconstituted with FAD, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol
Thermus thermophilus
4.95
-
purified recombinant apo-enzyme reconstituted with FMN, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol
Thermus thermophilus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
L-proline + 2,6-dichlorphenol-indophenol
-
743834
Thermus thermophilus
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + 2,6-dichlorphenol-indophenol
-
743834
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + a quinone
the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2
743834
Thermus thermophilus
(S)-1-pyrroline-5-carboxylate + a quinol
-
-
-
ir
L-proline + a quinone
the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2
743834
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
(S)-1-pyrroline-5-carboxylate + a quinol
-
-
-
ir
Subunits
Subunits
Commentary
Organism
dimer
2 * 74401, recombinant MBP-tagged enzyme, sequence calculation, 2 * 71899, recombinant enzyme mutant DELTAABC, sequence calculation
Thermus thermophilus
Synonyms
Synonyms
Commentary
Organism
TtProDH
-
Thermus thermophilus
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Thermus thermophilus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
7.2
-
L-proline
recombinant apo-enzyme reconstituted with FAD, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol
Thermus thermophilus
7.9
-
L-proline
recombinant apo-enzyme reconstituted with FMN, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol
Thermus thermophilus
9.8
-
L-proline
recombinant holo-enzyme, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol
Thermus thermophilus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.4
-
assay at
Thermus thermophilus
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
proline dehydrogenase from Thermus thermophilus does not discriminate between FAD and FMN as cofactor, redox active prosthetic group
Thermus thermophilus
FMN
proline dehydrogenase from Thermus thermophilus does not discriminate between FAD and FMN as cofactor, redox active prosthetic group
Thermus thermophilus
additional information
the recombinant holo form of MBP-tagged TtProDH, as produced in Escherichia coli TOP10 cells, contains about three times more FMN than FAD. The crystal structure of TtProDH variant DELTAABC, which lacks helices alphaA, alphaB and alphaC, shows no electron density for an AMP moiety of the cofactor. ProDH adopts a distorted (betalpha)8 TIM-barrel fold and is the only known TIM-barrel enzyme that contains an FAD cofactor. One cofactor molecule per enzyme subunit
Thermus thermophilus
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinant expression of the holo form of MBP-tagged TtProDH in Escherichia coli TOP10 cells, the recombinant enzyme contains about three times more FMN than FAD. The apoenzyme is produced by riboflavin auxotrophic Escherichia coli strain BSV11 and can be successfully reconstituted with FAD or FMN. The recombinant apo-enzyme reconstituted with FAD or FMN shows equal specific activities as holo-enzyme
Thermus thermophilus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
proline dehydrogenase from Thermus thermophilus does not discriminate between FAD and FMN as cofactor, redox active prosthetic group
Thermus thermophilus
FMN
proline dehydrogenase from Thermus thermophilus does not discriminate between FAD and FMN as cofactor, redox active prosthetic group
Thermus thermophilus
additional information
the recombinant holo form of MBP-tagged TtProDH, as produced in Escherichia coli TOP10 cells, contains about three times more FMN than FAD. The crystal structure of TtProDH variant DELTAABC, which lacks helices alphaA, alphaB and alphaC, shows no electron density for an AMP moiety of the cofactor. ProDH adopts a distorted (betalpha)8 TIM-barrel fold and is the only known TIM-barrel enzyme that contains an FAD cofactor. One cofactor molecule per enzyme subunit
Thermus thermophilus
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified TtProDH mutant variant DELTAABC lacking helices alphaA, alphaB and alphaC, X-ray diffraction structure determination and analysis at 2.2 A resolution
Thermus thermophilus
Engineering (protein specific)
Protein Variants
Commentary
Organism
F10E/L12E
construction of a variant with a more polar N-terminus, mutant F10E/L12E, because Thermus thermophilus ProDH (TtProDH), produced through fusion with maltose-binding protein (MBP) appears to be prone to aggregation. Preparation of TtProDH mutant variant DELTAABC, which lacks helices alphaA, alphaB and alphaC, the mutant shows no electron density for an AMP moiety of the cofactor
Thermus thermophilus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
36.6
-
L-proline
recombinant apo-enzyme reconstituted with FAD, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol
Thermus thermophilus
50.1
-
L-proline
recombinant apo-enzyme reconstituted with FMN, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol
Thermus thermophilus
76.6
-
L-proline
recombinant holo-enzyme, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol
Thermus thermophilus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
L-proline + a quinone
Thermus thermophilus
the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2
(S)-1-pyrroline-5-carboxylate + a quinol
-
-
ir
L-proline + a quinone
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2
(S)-1-pyrroline-5-carboxylate + a quinol
-
-
ir
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.84
-
purified recombinant apo-enzyme, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol
Thermus thermophilus
4.74
-
purified recombinant holo-enzyme, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol
Thermus thermophilus
4.83
-
purified recombinant apo-enzyme reconstituted with FAD, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol
Thermus thermophilus
4.95
-
purified recombinant apo-enzyme reconstituted with FMN, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol
Thermus thermophilus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
L-proline + 2,6-dichlorphenol-indophenol
-
743834
Thermus thermophilus
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + 2,6-dichlorphenol-indophenol
-
743834
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + a quinone
the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2
743834
Thermus thermophilus
(S)-1-pyrroline-5-carboxylate + a quinol
-
-
-
ir
L-proline + a quinone
the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2
743834
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
(S)-1-pyrroline-5-carboxylate + a quinol
-
-
-
ir
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 74401, recombinant MBP-tagged enzyme, sequence calculation, 2 * 71899, recombinant enzyme mutant DELTAABC, sequence calculation
Thermus thermophilus
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Thermus thermophilus
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
7.2
-
L-proline
recombinant apo-enzyme reconstituted with FAD, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol
Thermus thermophilus
7.9
-
L-proline
recombinant apo-enzyme reconstituted with FMN, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol
Thermus thermophilus
9.8
-
L-proline
recombinant holo-enzyme, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol
Thermus thermophilus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.4
-
assay at
Thermus thermophilus
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
146
-
L-proline
recombinant holo-enzyme, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol
Thermus thermophilus
158
-
L-proline
recombinant apo-enzyme reconstituted with FMN, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol
Thermus thermophilus
198
-
L-proline
recombinant apo-enzyme reconstituted with FAD, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol
Thermus thermophilus
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
146
-
L-proline
recombinant holo-enzyme, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol
Thermus thermophilus
158
-
L-proline
recombinant apo-enzyme reconstituted with FMN, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol
Thermus thermophilus
198
-
L-proline
recombinant apo-enzyme reconstituted with FAD, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol
Thermus thermophilus
Other publictions for EC 1.5.5.2
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
743834
Huijbers
Proline dehydrogenase from Th ...
Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Sci. Rep.
7
43880
2017
-
-
1
1
1
-
-
3
-
-
-
2
-
6
-
-
-
-
-
-
4
-
4
1
1
1
-
-
3
1
-
-
3
-
-
-
-
-
1
3
1
1
-
-
-
-
3
-
-
-
2
-
-
-
-
-
-
4
-
4
1
1
-
-
3
1
-
-
-
-
-
-
-
3
3
741588
Hancock
Co-regulation of mitochondria ...
Homo sapiens, Mus musculus
Amino Acids
48
859-872
2016
-
-
2
-
1
-
12
-
2
-
-
-
-
4
-
-
1
-
-
-
-
-
-
-
4
2
-
-
-
2
-
-
2
-
-
-
-
-
2
2
-
1
-
-
12
-
-
2
-
-
-
-
-
-
1
-
-
-
-
-
-
2
-
-
-
2
-
-
-
-
6
6
-
-
-
741858
Cabassa-Hourton
Proteomic and functional anal ...
Arabidopsis thaliana
Biochem. J.
473
2623-2634
2016
-
-
-
-
1
-
-
-
3
-
-
-
-
5
-
-
1
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
3
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
1
1
-
-
741642
Wang
Molecular cloning and express ...
Jatropha curcas
Appl. Biochem. Biotechnol.
175
2413-2426
2015
-
-
1
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
6
-
-
-
2
2
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
2
-
-
-
-
-
-
-
1
1
2
2
1
-
-
742162
Huijbers
High yields of active Thermus ...
Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Biotechnol. J.
10
395-403
2015
-
1
1
-
-
-
1
-
1
-
3
2
-
5
-
-
1
-
-
-
1
-
6
1
2
1
-
2
-
1
-
-
1
-
-
-
-
1
1
1
-
-
-
-
1
-
-
1
-
3
2
-
-
-
1
-
-
1
-
6
1
1
-
2
-
1
-
-
-
-
1
1
-
-
-
740734
Moxley
Evidence for hysteretic substr ...
Escherichia coli
J. Biol. Chem.
289
3639-3651
2014
-
-
-
-
-
-
-
3
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
1
-
-
-
-
-
-
-
-
3
3
742487
Schertl
Biochemical characterization ...
Arabidopsis thaliana
FEBS J.
281
2794-2804
2014
-
-
-
-
-
-
2
-
2
-
-
1
-
4
-
-
-
-
-
-
-
-
2
1
1
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
2
-
-
2
-
-
1
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
1
2
2
1
-
-
724389
Serrano
Kinetic and isotopic character ...
Mycobacterium tuberculosis
Biochemistry
52
5009-5015
2013
-
-
-
-
2
-
-
3
-
-
1
-
-
2
-
-
1
-
-
-
-
-
1
1
3
-
-
-
2
-
-
-
1
-
-
-
-
-
-
1
-
2
-
-
-
-
3
-
-
1
-
-
-
-
1
-
-
-
-
1
1
-
-
-
2
-
-
-
-
-
-
-
-
2
2
741732
Kawakami
Comparative analysis of the c ...
Pyrococcus furiosus, Pyrococcus horikoshii, Pyrococcus horikoshii OT-3, Thermococcus kodakarensis, Thermococcus kodakarensis KOD1 JCM12380, Thermococcus profundus, Thermococcus profundus DSM 9503
Appl. Microbiol. Biotechnol.
97
3419-3427
2013
-
-
4
-
-
-
8
-
-
-
-
-
-
13
-
-
4
-
-
-
-
-
22
7
24
4
-
4
-
4
-
-
4
-
-
-
-
-
7
7
-
-
-
-
14
-
-
-
-
-
-
-
-
-
7
-
-
-
-
22
7
7
-
7
-
7
-
-
-
-
8
14
-
-
-
742641
Omidinia
Expression, purification and ...
Pseudomonas putida, Pseudomonas putida POS-F84
Indian J. Microbiol.
53
297-302
2013
-
-
1
-
1
-
-
-
-
-
-
-
-
5
-
-
1
-
-
-
-
-
2
2
3
1
1
-
-
1
1
-
1
-
-
-
-
-
1
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
2
2
1
1
-
-
1
1
-
-
-
1
1
-
-
-
743635
Paes
Proline dehydrogenase regulat ...
Trypanosoma cruzi, Trypanosoma cruzi CL Brener
PLoS ONE
8
e69419
2013
-
-
1
-
-
-
-
1
1
-
-
2
-
5
-
-
1
-
-
1
-
-
10
1
4
1
-
-
-
1
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
1
1
-
-
2
-
-
-
1
-
1
-
-
10
1
1
-
-
-
1
-
-
-
1
2
2
1
-
-
724345
Moxley
Rapid reaction kinetics of pro ...
Escherichia coli
Biochemistry
51
511-520
2012
-
-
-
-
-
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
1
-
-
-
1
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
739932
Kawakami
L-proline dehydrogenases in hy ...
Pyrococcus horikoshii
Appl. Microbiol. Biotechnol.
93
83-93
2012
-
-
-
-
-
-
-
1
-
-
3
1
-
5
-
-
-
-
-
-
1
-
1
1
2
-
-
1
-
-
-
-
4
-
-
-
-
-
-
4
-
-
-
-
-
-
1
-
-
3
1
-
-
-
-
-
-
1
-
1
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
711252
Srivastava
The structure of the proline u ...
Escherichia coli
Biochemistry
49
560-569
2010
-
-
1
1
-
-
1
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
696361
Ostrander
A conserved active site tyrosi ...
Escherichia coli
Biochemistry
48
951-959
2009
-
-
1
1
2
-
1
6
-
-
-
-
-
3
-
-
1
-
-
-
-
-
2
-
1
-
-
-
6
-
-
-
1
3
-
-
-
-
1
1
1
2
-
-
1
3
6
-
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
671977
Zhu
Exploring the proline-dependen ...
Escherichia coli
Biochemistry
44
12297-12306
2005
-
-
-
-
4
-
-
4
1
-
-
-
-
2
-
-
-
1
-
-
-
-
1
-
1
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
4
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
658033
Zhang
Structures of the Escherichia ...
Escherichia coli
Biochemistry
43
12539-12548
2004
-
-
1
1
1
-
3
2
-
-
1
1
-
3
-
-
1
-
-
-
-
-
1
-
2
-
-
1
2
-
-
-
-
3
-
-
-
-
1
-
1
1
-
-
3
3
2
-
-
1
1
-
-
-
1
-
-
-
-
1
-
-
-
1
2
-
-
-
-
-
-
-
-
-
-
658211
Baban
Probing a hydrogen bond pair a ...
Escherichia coli
Biochim. Biophys. Acta
1701
49-59
2004
-
-
1
-
3
-
-
4
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
2
-
-
-
4
-
-
-
-
-
-
-
-
-
1
-
-
3
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
658668
Kawakami
Gene and primary structures of ...
Thermococcus profundus
Extremophiles
8
99-108
2004
-
-
1
-
-
-
-
1
-
1
5
-
-
10
-
-
1
-
-
-
1
-
2
1
1
1
-
1
-
1
-
1
1
-
-
-
-
-
1
1
-
-
-
-
-
-
1
-
1
5
-
-
-
-
1
-
-
1
-
2
1
1
-
1
-
1
-
1
-
-
-
-
-
-
-
659987
Lee
Structure of the proline dehyd ...
Escherichia coli
Nat. Struct. Biol.
10
109-114
2003
-
-
-
1
-
-
-
-
-
-
-
1
-
3
-
-
-
-
-
-
-
-
1
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
392565
Nadaraia
Crystallization and preliminar ...
Escherichia coli
Acta Crystallogr. Sect. D
57
1925-1927
2001
-
-
-
1
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
392570
Sakuraba
Purification, characterization ...
Thermococcus profundus
Appl. Environ. Microbiol.
67
1470-1475
2001
-
-
-
-
-
-
-
1
-
-
3
-
-
6
-
-
1
-
-
-
-
-
1
1
1
-
-
2
-
-
-
1
1
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
3
-
-
-
-
1
-
-
-
-
1
1
-
-
2
-
-
-
1
-
-
-
-
-
-
-
392572
Chaudhary
-
Proline dehydrogenase activity ...
Vigna radiata
Indian J. Exp. Biol.
37
1234-1240
1999
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
392571
Brown
Conformational change and memb ...
Escherichia coli
J. Biol. Chem.
268
8972-8979
1993
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
392569
Deutch
-
Oxidation of L-thiazolidine-4- ...
Escherichia coli
J. Gen. Microbiol.
138
1593-1598
1992
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
722591
Brown
Redesigned purification yields ...
Escherichia coli
J. Biol. Chem.
267
13086-13092
1992
-
-
-
-
-
-
-
-
-
-
2
1
-
3
-
-
1
-
-
-
1
-
1
1
2
1
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
2
1
-
-
-
1
-
-
1
-
1
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
392555
Wood
Membrane association of prolin ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
84
373-377
1987
-
-
1
-
-
-
-
-
2
-
-
1
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
392556
Graham
Proline dehydrogenase from Esc ...
Escherichia coli
J. Biol. Chem.
259
2656-2661
1984
-
-
-
-
-
-
2
2
2
-
-
1
-
4
-
-
1
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
2
-
2
2
-
-
1
-
-
-
1
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
392560
Scarpulla
Membrane-bound proline dehydro ...
Escherichia coli
J. Biol. Chem.
253
5997-6001
1978
-
-
-
-
-
-
5
1
1
-
1
1
-
2
-
-
1
-
-
-
1
-
4
1
-
-
-
-
-
1
-
-
1
4
-
-
-
-
-
1
-
-
-
-
5
4
1
1
-
1
1
-
-
-
1
-
-
1
-
4
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-