Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

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

Cloned(Commentary)

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.6.1.1 2-mercaptoethanol
-
Escherichia coli
1.6.1.1 beta-mercaptoethanol 72% residual activity at 0.2% (v/v) Escherichia coli
1.6.1.1 Ca2+ 91.2% residual activity at 2 mM; slightly inhibitory Escherichia coli
1.6.1.1 Co2+
-
Escherichia coli
1.6.1.1 Cu2+ complete inhibition at 2 mM Escherichia coli
1.6.1.1 dithiothreitol 75.3% residual activity at 2 mM Escherichia coli
1.6.1.1 DMSO slightly inhibitory Escherichia coli
1.6.1.1 DTT
-
Escherichia coli
1.6.1.1 EDTA 72.6% residual activity at 2 mM Escherichia coli
1.6.1.1 Mn2+ 67% residual activity at 2 mM Escherichia coli
1.6.1.1 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
1.6.1.1 NADPH EcSTH activity is strongly inhibited by excess NADPH, but not by thio-NAD+; the enzyme is strongly inhibited by excess NADPH Escherichia coli
1.6.1.1 Ni2+ 7.4% residual activity at 2 mM Escherichia coli
1.6.1.1 Zn2+ 10.1% residual activity at 2 mM Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.6.1.1 0.06829
-
NADPH at pH 7.5 and 35°C Escherichia coli
1.6.1.1 0.0683
-
NADPH pH 7.5, 35°C Escherichia coli
1.6.1.1 0.1332
-
thio-NAD+ pH 7.5, 35°C Escherichia coli
1.6.1.1 0.1332
-
thio-NAD+ at pH 7.5 and 35°C Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.6.1.1 soluble
-
Escherichia coli
-
-

Metals/Ions

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.6.1.1 51500
-
x * 51500, calculated from amino acid sequence Escherichia coli
1.6.1.1 52000
-
x * 52000, SDS-PAGE Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

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

Purification (Commentary)

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

Storage Stability

EC Number Storage Stability Organism
1.6.1.1 25°C, purified enzyme, 25 days, 65% activity remaining Escherichia coli
1.6.1.1 4°C, purified enzyme, 25 days, stable Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.6.1.1 NADPH + NAD+
-
Escherichia coli NADP+ + NADH
-
r
1.6.1.1 NADPH + thio-NAD+ + H+[side 1]
-
Escherichia coli NADP+ + thio-NADH + H+[side 2]
-
r
1.6.1.1 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

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

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.6.1.1 35
-
-
Escherichia coli

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.6.1.1 20 45 more than 70% activity between 20 and 45°C Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.6.1.1 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
1.6.1.1 50
-
purified enzyme, pH 7.5, 5h, 50% activity remaining, 80% activity remaining after 30 min Escherichia coli
1.6.1.1 57
-
purified enzyme, pH 7.5, 30 min, 50% activity remaining Escherichia coli
1.6.1.1 62
-
purified enzyme, pH 7.5, 30 min, 10% activity remaining Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.6.1.1 167.9
-
NADPH pH 7.5, 35°C Escherichia coli
1.6.1.1 167.9
-
NADPH at pH 7.5 and 35°C Escherichia coli
1.6.1.1 259.5
-
thio-NAD+ pH 7.5, 35°C Escherichia coli
1.6.1.1 259.5
-
thio-NAD+ at pH 7.5 and 35°C Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.6.1.1 7.5
-
-
Escherichia coli

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.6.1.1 7 9 more than 50% activity between pH 7.0 and 9.0 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.6.1.1 flavin flavoprotein Escherichia coli

General Information

EC Number General Information Comment Organism
1.6.1.1 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
1.6.1.1 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]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.6.1.1 1940
-
thio-NAD+ at pH 7.5 and 35°C Escherichia coli
1.6.1.1 2460
-
NADPH at pH 7.5 and 35°C Escherichia coli