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L-pipecolate + NAD+ = DELTA1-piperideine-2-carboxylate + NADH + H+
L-proline + NAD+ = DELTA1-pyrroline-2-carboxylate + NADH + H+
L-pipecolate + NAD+ = DELTA1-piperideine-2-carboxylate + NADH + H+
(1)
L-pipecolate + NAD+ = DELTA1-piperideine-2-carboxylate + NADH + H+
(1)
-
-
L-pipecolate + NAD+ = DELTA1-piperideine-2-carboxylate + NADH + H+
-
-
-
-
L-proline + NAD+ = DELTA1-pyrroline-2-carboxylate + NADH + H+
(2)
L-proline + NAD+ = DELTA1-pyrroline-2-carboxylate + NADH + H+
catalytic mechanism, overview. The hydride ion is transferred from the C4 atom of NADH to the C2 atom of Pyr2C, causing electron transfer to the vicinal N atom of Pyr2C, which is now capable of accepting the proton donated by the guanidine group of Arg43. The product L-proline forms a hydrogen bond to the carbonyl O atom of Val301, which stabilizes formation of the product prior to its release. Lys71 and Arg114 are highly conserved and are involved in substrate binding through their interaction with the substrate carboxyl group. But the NH2 group of the guanidine of Arg43 engages in a hydrogen bond to the close carbonyl O atom of Val301 and to the distant N atom of the substrate, the putative proton acceptor of the catalytic reaction
-
L-proline + NAD+ = DELTA1-pyrroline-2-carboxylate + NADH + H+
catalytic mechanism, overview. The hydride ion is transferred from the C4 atom of NADH to the C2 atom of Pyr2C, causing electron transfer to the vicinal N atom of Pyr2C, which is now capable of accepting the proton donated by the guanidine group of Arg43. The product L-proline forms a hydrogen bond to the carbonyl O atom of Val301, which stabilizes formation of the product prior to its release. Lys71 and Arg114 are highly conserved and are involved in substrate binding through their interaction with the substrate carboxyl group. But the NH2 group of the guanidine of Arg43 engages in a hydrogen bond to the close carbonyl O atom of Val301 and to the distant N atom of the substrate, the putative proton acceptor of the catalytic reaction
-
-
L-proline + NAD+ = DELTA1-pyrroline-2-carboxylate + NADH + H+
catalytic mechanism, overview. The hydride ion is transferred from the C4 atom of NADH to the C2 atom of Pyr2C, causing electron transfer to the vicinal N atom of Pyr2C, which is now capable of accepting the proton donated by the guanidine group of Arg43. The product L-proline forms a hydrogen bond to the carbonyl O atom of Val301, which stabilizes formation of the product prior to its release. Lys71 and Arg114 are highly conserved and are involved in substrate binding through their interaction with the substrate carboxyl group. But the NH2 group of the guanidine of Arg43 engages in a hydrogen bond to the close carbonyl O atom of Val301 and to the distant N atom of the substrate, the putative proton acceptor of the catalytic reaction
-
-
L-proline + NAD+ = DELTA1-pyrroline-2-carboxylate + NADH + H+
(2)
-
-
L-proline + NAD+ = DELTA1-pyrroline-2-carboxylate + NADH + H+
catalytic mechanism, overview. The hydride ion is transferred from the C4 atom of NADH to the C2 atom of Pyr2C, causing electron transfer to the vicinal N atom of Pyr2C, which is now capable of accepting the proton donated by the guanidine group of Arg43. The product L-proline forms a hydrogen bond to the carbonyl O atom of Val301, which stabilizes formation of the product prior to its release. Lys71 and Arg114 are highly conserved and are involved in substrate binding through their interaction with the substrate carboxyl group. But the NH2 group of the guanidine of Arg43 engages in a hydrogen bond to the close carbonyl O atom of Val301 and to the distant N atom of the substrate, the putative proton acceptor of the catalytic reaction
-
-
L-proline + NAD+ = DELTA1-pyrroline-2-carboxylate + NADH + H+
catalytic mechanism, overview. The hydride ion is transferred from the C4 atom of NADH to the C2 atom of Pyr2C, causing electron transfer to the vicinal N atom of Pyr2C, which is now capable of accepting the proton donated by the guanidine group of Arg43. The product L-proline forms a hydrogen bond to the carbonyl O atom of Val301, which stabilizes formation of the product prior to its release. Lys71 and Arg114 are highly conserved and are involved in substrate binding through their interaction with the substrate carboxyl group. But the NH2 group of the guanidine of Arg43 engages in a hydrogen bond to the close carbonyl O atom of Val301 and to the distant N atom of the substrate, the putative proton acceptor of the catalytic reaction
-
-
L-proline + NAD+ = DELTA1-pyrroline-2-carboxylate + NADH + H+
-
-
-
-
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1-pyrroline-2-carboxylate + NADH + H+
L-proline + NAD+
cis-4-hydroxy-L-proline + NAD+
?
cis-4-hydroxy-L-proline + NAD+
DELTA1-pyrroline-4S-hydroxy-2-carboxylate + NADPH + H+
DELTA1-pyrroline-2-carboxylate + NADH + H+
L-proline + NAD+
L-pipecolate + NAD+
1-piperideine-2-carboxylate + NADH + H+
L-pipecolate + NAD+
DELTA1-piperideine-2-carboxylate + NADH + H+
L-proline + NAD+
DELTA1-pyrroline-2-carboxylate + NADH + H+
trans-4-hydroxy-L-proline + NAD+
?
activity is 70% compared to the activity with L-proline
-
-
?
trans-4-hydroxy-L-proline + NAD+
DELTA1-pyrroline-4R-hydroxy-2-carboxylate + NADPH + H+
-
-
-
-
r
additional information
?
-
1-pyrroline-2-carboxylate + NADH + H+
L-proline + NAD+
-
-
-
-
r
1-pyrroline-2-carboxylate + NADH + H+
L-proline + NAD+
-
highly preferred substrates, preference of the reaction equilibrium in the direction toward NADH-dependent reduction
-
-
r
1-pyrroline-2-carboxylate + NADH + H+
L-proline + NAD+
-
-
-
-
r
1-pyrroline-2-carboxylate + NADH + H+
L-proline + NAD+
-
highly preferred substrates, preference of the reaction equilibrium in the direction toward NADH-dependent reduction
-
-
r
cis-4-hydroxy-L-proline + NAD+
?
activity is 85% compared to the activity with L-proline
-
-
?
cis-4-hydroxy-L-proline + NAD+
?
activity is 85% compared to the activity with L-proline
-
-
?
cis-4-hydroxy-L-proline + NAD+
DELTA1-pyrroline-4S-hydroxy-2-carboxylate + NADPH + H+
-
-
-
-
r
cis-4-hydroxy-L-proline + NAD+
DELTA1-pyrroline-4S-hydroxy-2-carboxylate + NADPH + H+
-
-
-
-
r
DELTA1-pyrroline-2-carboxylate + NADH + H+
L-proline + NAD+
the enzyme is involved in the trans-3-hydroxy-L-proline metabolism
-
-
?
DELTA1-pyrroline-2-carboxylate + NADH + H+
L-proline + NAD+
preference of the reaction equilibrium in the direction toward NADH-dependent reduction
-
-
r
DELTA1-pyrroline-2-carboxylate + NADH + H+
L-proline + NAD+
the enzyme is involved in the trans-3-hydroxy-L-proline metabolism
-
-
?
DELTA1-pyrroline-2-carboxylate + NADH + H+
L-proline + NAD+
preference of the reaction equilibrium in the direction toward NADH-dependent reduction
-
-
r
L-pipecolate + NAD+
1-piperideine-2-carboxylate + NADH + H+
-
-
-
-
r
L-pipecolate + NAD+
1-piperideine-2-carboxylate + NADH + H+
-
-
-
-
r
L-pipecolate + NAD+
DELTA1-piperideine-2-carboxylate + NADH + H+
activity is 49% compared to the activity with L-proline
-
-
?
L-pipecolate + NAD+
DELTA1-piperideine-2-carboxylate + NADH + H+
activity is 49% compared to the activity with L-proline
-
-
?
L-proline + NAD+
DELTA1-pyrroline-2-carboxylate + NADH + H+
-
-
-
-
r
L-proline + NAD+
DELTA1-pyrroline-2-carboxylate + NADH + H+
preference of the reaction equilibrium in the direction toward NADH-dependent reduction
-
-
r
L-proline + NAD+
DELTA1-pyrroline-2-carboxylate + NADH + H+
-
-
-
-
r
L-proline + NAD+
DELTA1-pyrroline-2-carboxylate + NADH + H+
-
-
-
-
r
L-proline + NAD+
DELTA1-pyrroline-2-carboxylate + NADH + H+
-
-
-
-
r
L-proline + NAD+
DELTA1-pyrroline-2-carboxylate + NADH + H+
-
-
-
-
r
additional information
?
-
the enzyme also shows alanine dehydrogenase activity (EC 1.4.1.1) and N-methyl-L-alanine dehydrogenase activity (EC 1.4.1.17)
-
-
?
additional information
?
-
-
the enzyme also shows alanine dehydrogenase activity (EC 1.4.1.1) and N-methyl-L-alanine dehydrogenase activity (EC 1.4.1.17)
-
-
?
additional information
?
-
-
trans-4-hydroxy-L-proline, L-2-aminovalerate, and N-methyl-L-alanine. TlLhpI shows NAD+-dependent oxidation of L-proline. The kcat/Km value in the presence of NADP+ is about 50fold lower than that in the presence of NAD+. In addition to L-proline, several L-proline analogues, including cis-4-hydroxy-L-proline (85%), trans-4-hydroxy-L-proline (70%), and L-pipecolate (49%), are active substrates (relative activity to L-proline in parentheses). The enzyme also shows low activity with pyruvate, oxaloacetate, 2-oxobutyrate, 2-oxovalerate, and 4-methyl-2-oxovalerate in the oxidation reaction direction, overview
-
-
?
additional information
?
-
-
trans-4-hydroxy-L-proline, L-2-aminovalerate, and N-methyl-L-alanine. TlLhpI shows NAD+-dependent oxidation of L-proline. The kcat/Km value in the presence of NADP+ is about 50fold lower than that in the presence of NAD+. In addition to L-proline, several L-proline analogues, including cis-4-hydroxy-L-proline (85%), trans-4-hydroxy-L-proline (70%), and L-pipecolate (49%), are active substrates (relative activity to L-proline in parentheses). The enzyme also shows low activity with pyruvate, oxaloacetate, 2-oxobutyrate, 2-oxovalerate, and 4-methyl-2-oxovalerate in the oxidation reaction direction, overview
-
-
?
additional information
?
-
the enzyme also shows alanine dehydrogenase activity (EC 1.4.1.1) and N-methyl-L-alanine dehydrogenase activity (EC 1.4.1.17)
-
-
?
additional information
?
-
-
the enzyme also shows alanine dehydrogenase activity (EC 1.4.1.1) and N-methyl-L-alanine dehydrogenase activity (EC 1.4.1.17)
-
-
?
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1-pyrroline-2-carboxylate + NADH + H+
L-proline + NAD+
DELTA1-pyrroline-2-carboxylate + NADH + H+
L-proline + NAD+
L-proline + NAD+
DELTA1-pyrroline-2-carboxylate + NADH + H+
1-pyrroline-2-carboxylate + NADH + H+
L-proline + NAD+
-
-
-
-
r
1-pyrroline-2-carboxylate + NADH + H+
L-proline + NAD+
-
-
-
-
r
DELTA1-pyrroline-2-carboxylate + NADH + H+
L-proline + NAD+
the enzyme is involved in the trans-3-hydroxy-L-proline metabolism
-
-
?
DELTA1-pyrroline-2-carboxylate + NADH + H+
L-proline + NAD+
the enzyme is involved in the trans-3-hydroxy-L-proline metabolism
-
-
?
L-proline + NAD+
DELTA1-pyrroline-2-carboxylate + NADH + H+
-
-
-
-
r
L-proline + NAD+
DELTA1-pyrroline-2-carboxylate + NADH + H+
-
-
-
-
r
L-proline + NAD+
DELTA1-pyrroline-2-carboxylate + NADH + H+
-
-
-
-
r
L-proline + NAD+
DELTA1-pyrroline-2-carboxylate + NADH + H+
-
-
-
-
r
L-proline + NAD+
DELTA1-pyrroline-2-carboxylate + NADH + H+
-
-
-
-
r
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0.944 - 2.77
1-pyrroline-2-carboxylate
0.944 - 2.77
DELTA1-pyrroline-2-carboxylate
0.608
L-pipecolate
pH 6.0, 50°C, wild-type enzyme
0.944
1-pyrroline-2-carboxylate
-
recombinant wild-type enzyme, pH 6.5, 50°C, with NADH
2.77
1-pyrroline-2-carboxylate
-
recombinant mutant V224D/A228K enzyme, pH 6.5, 50°C, with NADH
0.944
DELTA1-pyrroline-2-carboxylate
pH 6.0, 50°C, wild-type enzyme
2.77
DELTA1-pyrroline-2-carboxylate
pH 6.0, 50°C, mutant enzyme V224D/A228K
0.444
L-proline
pH 6.0, 50°C, mutant enzyme V224D/A228K
1.12
L-proline
pH 6.0, 50°C, wild-type enzyme
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16.58 - 558.3
1-pyrroline-2-carboxylate
16.6 - 558
DELTA1-pyrroline-2-carboxylate
0.2
L-pipecolate
pH 6.0, 50°C, wild-type enzyme
16.58
1-pyrroline-2-carboxylate
-
recombinant wild-type enzyme, pH 6.5, 50°C, with NADH
558.3
1-pyrroline-2-carboxylate
-
recombinant mutant V224D/A228K enzyme, pH 6.5, 50°C, with NADH
16.6
DELTA1-pyrroline-2-carboxylate
pH 6.0, 50°C, wild-type enzyme
558
DELTA1-pyrroline-2-carboxylate
pH 6.0, 50°C, mutant enzyme V224D/A228K
0.23
L-proline
pH 6.0, 50°C, wild-type enzyme
0.61
L-proline
pH 6.0, 50°C, mutant enzyme V224D/A228K
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17.57 - 201.6
1-pyrroline-2-carboxylate
17.6 - 201
DELTA1-pyrroline-2-carboxylate
0.33
L-pipecolate
pH 6.0, 50°C, wild-type enzyme
17.57
1-pyrroline-2-carboxylate
-
recombinant wild-type enzyme, pH 6.5, 50°C, with NADH
201.6
1-pyrroline-2-carboxylate
-
recombinant mutant V224D/A228K enzyme, pH 6.5, 50°C, with NADH
17.6
DELTA1-pyrroline-2-carboxylate
pH 6.0, 50°C, wild-type enzyme
201
DELTA1-pyrroline-2-carboxylate
pH 6.0, 50°C, mutant enzyme V224D/A228K
0.2
L-proline
pH 6.0, 50°C, wild-type enzyme
1.4
L-proline
pH 6.0, 50°C, mutant enzyme V224D/A228K
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evolution
-
the enzyme belongs to the ornithine cyclodeaminase/l-crystallin (OCD/CRYM) superfamily
evolution
-
the enzyme belongs to the ornithine cyclodeaminase/l-crystallin (OCD/CRYM) superfamily
-
metabolism
the enzyme is involved in the trans-3-hydroxy-L-proline metabolism
metabolism
-
the enzyme performs the second step of the trans-3-hydroxy-L-proline (T3LHyp) degradation pathway
metabolism
-
the enzyme performs the second step of the trans-3-hydroxy-L-proline (T3LHyp) degradation pathway
-
metabolism
-
the enzyme performs the second step of the trans-3-hydroxy-L-proline (T3LHyp) degradation pathway
-
metabolism
-
the enzyme is involved in the trans-3-hydroxy-L-proline metabolism
-
metabolism
-
the enzyme performs the second step of the trans-3-hydroxy-L-proline (T3LHyp) degradation pathway
-
metabolism
-
the enzyme performs the second step of the trans-3-hydroxy-L-proline (T3LHyp) degradation pathway
-
physiological function
-
approximately 40% of L-proline in collagen are post-translationally converted by proline hydroxylases into the isomers trans-4-hydroxy-L-proline (T4LHyp) and trans-3-hydroxy-L-proline (T3LHyp). The isomers trans-3-hydroxy-L-proline (T3LHyp) and trans-4-hydroxy-L-proline (T4LHyp) are major components of mammalian collagen. T4LHyp follows two distinct degradation pathways in bacteria and mammals, while T3LHyp is metabolized by a two-step metabolic pathway that is conserved in bacteria and mammals, which involves a T3LHyp dehydratase and a DELTA1-pyrroline-2-carboxylate (Pyr2C) reductase
physiological function
-
approximately 40% of L-proline in collagen are post-translationally converted by proline hydroxylases into the isomers trans-4-hydroxy-L-proline (T4LHyp) and trans-3-hydroxy-L-proline (T3LHyp). The isomers trans-3-hydroxy-L-proline (T3LHyp) and trans-4-hydroxy-L-proline (T4LHyp) are major components of mammalian collagen. T4LHyp follows two distinct degradation pathways in bacteria and mammals, while T3LHyp is metabolized by a two-step metabolic pathway that is conserved in bacteria and mammals, which involves a T3LHyp dehydratase and a DELTA1-pyrroline-2-carboxylate (Pyr2C) reductase
-
physiological function
-
approximately 40% of L-proline in collagen are post-translationally converted by proline hydroxylases into the isomers trans-4-hydroxy-L-proline (T4LHyp) and trans-3-hydroxy-L-proline (T3LHyp). The isomers trans-3-hydroxy-L-proline (T3LHyp) and trans-4-hydroxy-L-proline (T4LHyp) are major components of mammalian collagen. T4LHyp follows two distinct degradation pathways in bacteria and mammals, while T3LHyp is metabolized by a two-step metabolic pathway that is conserved in bacteria and mammals, which involves a T3LHyp dehydratase and a DELTA1-pyrroline-2-carboxylate (Pyr2C) reductase
-
physiological function
-
approximately 40% of L-proline in collagen are post-translationally converted by proline hydroxylases into the isomers trans-4-hydroxy-L-proline (T4LHyp) and trans-3-hydroxy-L-proline (T3LHyp). The isomers trans-3-hydroxy-L-proline (T3LHyp) and trans-4-hydroxy-L-proline (T4LHyp) are major components of mammalian collagen. T4LHyp follows two distinct degradation pathways in bacteria and mammals, while T3LHyp is metabolized by a two-step metabolic pathway that is conserved in bacteria and mammals, which involves a T3LHyp dehydratase and a DELTA1-pyrroline-2-carboxylate (Pyr2C) reductase
-
physiological function
-
approximately 40% of L-proline in collagen are post-translationally converted by proline hydroxylases into the isomers trans-4-hydroxy-L-proline (T4LHyp) and trans-3-hydroxy-L-proline (T3LHyp). The isomers trans-3-hydroxy-L-proline (T3LHyp) and trans-4-hydroxy-L-proline (T4LHyp) are major components of mammalian collagen. T4LHyp follows two distinct degradation pathways in bacteria and mammals, while T3LHyp is metabolized by a two-step metabolic pathway that is conserved in bacteria and mammals, which involves a T3LHyp dehydratase and a DELTA1-pyrroline-2-carboxylate (Pyr2C) reductase
-
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N168A
-
site-directed mutagenesis
R43A
-
site-directed mutagenesis
N168A
-
site-directed mutagenesis
-
R43A
-
site-directed mutagenesis
-
N168A
-
site-directed mutagenesis
-
R43A
-
site-directed mutagenesis
-
N168A
-
site-directed mutagenesis
-
R43A
-
site-directed mutagenesis
-
N168A
-
site-directed mutagenesis
-
R43A
-
site-directed mutagenesis
-
L52E/V224D/A228K
DELTA1-pyrroline-2-carboxylate reductase activity is the same as in wild-type enzyme, no alanine dehydrogenase activity
L52E/V224D/A228K
-
site-directed mutagenesis, the mutant shows 2fold increased activity and highly increased specifiicity for substrate DELTA1-pyrrolidine-2-carboxylate as compared to the wild-type enzyme
L52R/V224D/A228K
DELTA1-pyrroline-2-carboxylate reductase activity is the same as in wild-type enzyme, no alanine dehydrogenase activity
L52R/V224D/A228K
-
site-directed mutagenesis, the mutant shows slightly increased activity and highly increased specifiicity for substrate DELTA1-pyrrolidine-2-carboxylate and no activity with other substrates in contrast to the wild-type enzyme
V224D/A228K
12fold enhancement of DELTA1-pyrroline-2-carboxylate reductase activity, 6.7fold enhancement for the oxidization activity for L-proline, no alanine dehydrogenase activity
V224D/A228K
-
site-directed mutagenesis, the mutant shows 10fold increased activity for substrate DELTA1-pyrrolidine-2-carboxylate as compared to the wild-type enzyme
L52E/V224D/A228K
-
site-directed mutagenesis, the mutant shows 2fold increased activity and highly increased specifiicity for substrate DELTA1-pyrrolidine-2-carboxylate as compared to the wild-type enzyme
-
L52E/V224D/A228K
-
DELTA1-pyrroline-2-carboxylate reductase activity is the same as in wild-type enzyme, no alanine dehydrogenase activity
-
L52R/V224D/A228K
-
site-directed mutagenesis, the mutant shows slightly increased activity and highly increased specifiicity for substrate DELTA1-pyrrolidine-2-carboxylate and no activity with other substrates in contrast to the wild-type enzyme
-
L52R/V224D/A228K
-
DELTA1-pyrroline-2-carboxylate reductase activity is the same as in wild-type enzyme, no alanine dehydrogenase activity
-
V224D/A228K
-
site-directed mutagenesis, the mutant shows 10fold increased activity for substrate DELTA1-pyrrolidine-2-carboxylate as compared to the wild-type enzyme
-
V224D/A228K
-
12fold enhancement of DELTA1-pyrroline-2-carboxylate reductase activity, 6.7fold enhancement for the oxidization activity for L-proline, no alanine dehydrogenase activity
-
additional information
TlLhpI is a fusion of OCC_00362 and OCC_00367 genes by PCR. The gene from Thermococcus litoralis DSM 5473 consistsof two separate open-reading frames (ORFs): OCC_00362 and OCC_00367. When a single A is inserted between A227646 and T227647 in the original genome sequence of T. litoralis DSM 5473, the separate ORFs fuse into a single ORF, and the putative amino acid sequence of is homologous to that of the Thermococcus sibiricus TSIB_0634 gene. Although there is a possibility that this OCD-like protein from Thermococcus litoralis DSM 5473 forms a heterooligomeric structure, the TlLhpI gene is synthesized as a single ORF by sequential steps of PCR using sense and antisense primers and genome DNA of Thermococcus litoralis DSM 5473 as a template
additional information
-
TlLhpI is a fusion of OCC_00362 and OCC_00367 genes by PCR. The gene from Thermococcus litoralis DSM 5473 consistsof two separate open-reading frames (ORFs): OCC_00362 and OCC_00367. When a single A is inserted between A227646 and T227647 in the original genome sequence of T. litoralis DSM 5473, the separate ORFs fuse into a single ORF, and the putative amino acid sequence of is homologous to that of the Thermococcus sibiricus TSIB_0634 gene. Although there is a possibility that this OCD-like protein from Thermococcus litoralis DSM 5473 forms a heterooligomeric structure, the TlLhpI gene is synthesized as a single ORF by sequential steps of PCR using sense and antisense primers and genome DNA of Thermococcus litoralis DSM 5473 as a template
additional information
-
TlLhpI is a fusion of OCC_00362 and OCC_00367 genes by PCR. The gene from Thermococcus litoralis DSM 5473 consistsof two separate open-reading frames (ORFs): OCC_00362 and OCC_00367. When a single A is inserted between A227646 and T227647 in the original genome sequence of T. litoralis DSM 5473, the separate ORFs fuse into a single ORF, and the putative amino acid sequence of is homologous to that of the Thermococcus sibiricus TSIB_0634 gene. Although there is a possibility that this OCD-like protein from Thermococcus litoralis DSM 5473 forms a heterooligomeric structure, the TlLhpI gene is synthesized as a single ORF by sequential steps of PCR using sense and antisense primers and genome DNA of Thermococcus litoralis DSM 5473 as a template
-
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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 (H3ZMH3 and H3ZMH4), Thermococcus litoralis, Thermococcus litoralis DSM 5473 (H3ZMH3 and H3ZMH4), Thermococcus litoralis DSM 5473
brenda
Watanabe, S.; Tozawa, Y.; Watanabe, Y.
Ornithine cyclodeaminase/micro-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, Thermococcus litoralis DSM 5473
brenda
Ferrario, E.; Miggiano, R.; Rizzi, M.; Ferraris, D.M.
Structure of Thermococcus litoralis DELTA1-pyrroline-2-carboxylate reductase in complex with NADH and L-proline
Acta Crystallogr. Sect. D
76
496-505
2020
Thermococcus litoralis, Thermococcus litoralis JCM 8560, Thermococcus litoralis DSM 5473, Thermococcus litoralis ATCC 51850, Thermococcus litoralis NS-C
brenda
1.5.1.B5 DELTA1-piperideine-2-carboxylate/DELTA1-pyrroline-2-carboxylate reductase (NADH)
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