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Literature summary for 1.6.1.1 extracted from

  • Cao, Z.; Song, P.; Xu, Q.; Su, R.; Zhu, G.
    Overexpression and biochemical characterization of soluble pyridine nucleotide transhydrogenase from Escherichia coli (2011), FEMS Microbiol. Lett., 320, 9-14.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
ADP 75.5% activation at 2 mM Escherichia coli
ADP 175.5% activity at 2 mM ADP Escherichia coli
AMP 71.8% activation at 2 mM Escherichia coli
AMP 171.8% activity at 2 mM AMP Escherichia coli
ATP 53.4% activation at 2 mM Escherichia coli
ATP 153.4% activity at 2 mM ATP Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli DH5alpha cells Escherichia coli
expression of the soluble enzyme in Escherichia coli strain DH5alpha Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
2-mercaptoethanol
-
Escherichia coli
beta-mercaptoethanol 72% residual activity at 0.2% (v/v) Escherichia coli
Ca2+ 91.2% residual activity at 2 mM; slightly inhibitory Escherichia coli
Co2+
-
Escherichia coli
Cu2+ complete inhibition at 2 mM Escherichia coli
dithiothreitol 75.3% residual activity at 2 mM Escherichia coli
DMSO slightly inhibitory Escherichia coli
DTT
-
Escherichia coli
EDTA 72.6% residual activity at 2 mM Escherichia coli
Mn2+ 67% residual activity at 2 mM Escherichia coli
additional information no or poor inhibition of the enzyme by Na+, Rb+, K+, Li+,, and Mg2+; the enzyme is not inhibited by thio-NAD+ and DMSO Escherichia coli
NADPH EcSTH activity is strongly inhibited by excess NADPH, but not by thio-NAD+; the enzyme is strongly inhibited by excess NADPH Escherichia coli
Ni2+ 7.4% residual activity at 2 mM Escherichia coli
Zn2+ 10.1% residual activity at 2 mM Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.06829
-
NADPH at pH 7.5 and 35°C Escherichia coli
0.0683
-
NADPH pH 7.5, 35°C Escherichia coli
0.1332
-
thio-NAD+ pH 7.5, 35°C Escherichia coli
0.1332
-
thio-NAD+ at pH 7.5 and 35°C Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
-
Escherichia coli
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
additional information not influenced by Na+, Rb+, K+, Li+, and Mg2+ Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
51500
-
x * 51500, calculated from amino acid sequence Escherichia coli
52000
-
x * 52000, SDS-PAGE Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
NADPH + NAD+ Escherichia coli
-
NADP+ + NADH
-
r

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli P27306 substrain MG1655, gene sth
-

Purification (Commentary)

Purification (Comment) Organism
TALON metal affinity resin column chromatography Escherichia coli

Storage Stability

Storage Stability Organism
25°C, purified enzyme, 25 days, 65% activity remaining Escherichia coli
4°C, purified enzyme, 25 days, stable Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NADPH + NAD+
-
Escherichia coli NADP+ + NADH
-
r
NADPH + thio-NAD+ + H+[side 1]
-
Escherichia coli NADP+ + thio-NADH + H+[side 2]
-
r
NADPH + thio-NAD+ + H+[side 1] EcSTH has a 1.25fold preference for NADPH over thio-NAD+ Escherichia coli NADP+ + thio-NADH + H+[side 2]
-
r

Subunits

Subunits Comment Organism
? x * 52000, SDS-PAGE Escherichia coli
? x * 51500, calculated from amino acid sequence Escherichia coli

Synonyms

Synonyms Comment Organism
energy-independent soluble pyridine nucleotide transhydrogenase
-
Escherichia coli
soluble pyridine nucleotide transhydrogenase
-
Escherichia coli
STH
-
Escherichia coli
UdhA
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
-
Escherichia coli

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
20 45 more than 70% activity between 20 and 45°C Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4 50 the enzyme retains 50% activity after 5 h at 50°C. The enzyme is stable at 4°C for 25 days and retains 65% activity at 25°C. The enzyme is rapidly inactivated at high temperatures, retaining 80%, 50% and 10% activity after incubation for 30 min at 50, 57 and 62°C, respectively Escherichia coli
50
-
purified enzyme, pH 7.5, 5h, 50% activity remaining, 80% activity remaining after 30 min Escherichia coli
57
-
purified enzyme, pH 7.5, 30 min, 50% activity remaining Escherichia coli
62
-
purified enzyme, pH 7.5, 30 min, 10% activity remaining Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
167.9
-
NADPH pH 7.5, 35°C Escherichia coli
167.9
-
NADPH at pH 7.5 and 35°C Escherichia coli
259.5
-
thio-NAD+ pH 7.5, 35°C Escherichia coli
259.5
-
thio-NAD+ at pH 7.5 and 35°C Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
7 9 more than 50% activity between pH 7.0 and 9.0 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
flavin flavoprotein Escherichia coli

General Information

General Information Comment Organism
evolution two pyridine nucleotide transhydrogenases: the energy-independent soluble pyridine nucleotide transhydrogenase (STH or UdhA) (EC 1.6.1.1) and the membrane-bound, energy-dependent pyridine nucleotide transhydrogenase (TH or PntAB) (EC 1.6.1.2). PntAB is widely distributed in the mitochondria and some bacteria, while STH is found only in certain Gammaproteobacteria and gram-positive bacteria Escherichia coli
physiological function the soluble pyridine nucleotide transhydrogenase, STH, is an energy-independent flavoprotein that directly catalyzes hydride transfer between NAD(H) and NADP(H) to maintain homeostasis of these two redox cofactors Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1940
-
thio-NAD+ at pH 7.5 and 35°C Escherichia coli
2460
-
NADPH at pH 7.5 and 35°C Escherichia coli