1.1.1.145: 3beta-hydroxy-DELTA5-steroid dehydrogenase

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For detailed information about 3beta-hydroxy-DELTA5-steroid dehydrogenase, go to the full flat file.

Reaction

Synonyms

3 beta- and steroid deltaisomerase 1, 3-beta-hydroxy-5-ene steroid dehydrogenase, 3-beta-hydroxy-delta(5)-steroid dehydrogenase, 3-beta-hydroxysteroid dehydrogenase, 3-beta-hydroxysteroid dehydrogenase type-2, 3beta hydroxysteroid dehydrogenase, 3beta-HSD, 3beta-HSD type II, 3beta-HSD1, 3beta-HSD2, 3beta-HSD22, 3beta-HSDH, 3beta-HSD_1, 3beta-hydroxy steroid dehydrogenase/5-ene-4-ene isomerase, 3beta-hydroxy steroid dehydrogenase/isomerase, 3beta-hydroxy-5-ene steroid dehydrogenase, 3beta-hydroxy-5-ene-steroid dehydrogenase, 3beta-hydroxy-5-ene-steroid oxidoreductase, 3beta-hydroxy-DELTA5-C27-steroid dehydrogenase/isomerase, 3beta-hydroxy-DELTA5-C27-steroid oxidoreductase, 3beta-hydroxysteroid dehydrogenase, 3beta-hydroxysteroid dehydrogenase 1, 3beta-hydroxysteroid dehydrogenase 2, 3beta-hydroxysteroid dehydrogenase type 1, 3beta-hydroxysteroid dehydrogenase type 2, 3beta-hydroxysteroid dehydrogenase type 2 and, 3beta-hydroxysteroid dehydrogenase type II, 3beta-hydroxysteroid dehydrogenase type1, 3beta-hydroxysteroid dehydrogenase/3-ketosteroid reductase, 3beta-hydroxysteroid dehydrogenase/DELTA5-DELAT4 isomerase type 2, 3beta-hydroxysteroid dehydrogenase/DELTA5-DELTA4 isomerase, 3beta-hydroxysteroid dehydrogenase/DELTA5-DELTA4-isomerase, 3beta-hydroxysteroid dehydrogenase/DELTA5-DELTA4-isomerase type II, 3beta-hydroxysteroid dehydrogenase/isomerase, 3beta-hydroxysteroid dehydrogenase/isomerase type 1, 3beta-hydroxysteroid dehydrogenase/steroid DELTA5,4-isomerase, 3betaHSD, 3betaHSD1, 3betaHSD2, 5-ene-3-beta-hydroxysteroid dehydrogenase, 5alpha-dihydrotestosterone 3beta-hydroxysteroid dehydrogenase, dehydrogenase, 3beta-hydroxy-DELTA5-steroid, DELTA5-3beta-hydroxysteroid dehydrogenase, DHRS4, HSD2, HSD3B, HSD3B1, HSD3B2, Hsd3b6, HSDB1, HSDH, More, progesterone reductase, Sl3betaHSD1, Solyc01g73640, steroid-DELTA5-3beta-ol dehydrogenase, type 1 3beta-hydroxysteroid dehydrogenase, type 1 3beta-hydroxysteroid dehydrogenase/isomerase, type 2 3beta-hydroxysteroid dehydrogenase, type 2 3beta-hydroxysteroid dehydrogenase/isomerase

ECTree

     1 Oxidoreductases

         1.1 Acting on the CH-OH group of donors

             1.1.1 With NAD⁺ or NADP⁺ as acceptor

                1.1.1.145 3beta-hydroxy-DELTA5-steroid dehydrogenase

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Results	in table
6	Activating Compound
110	AA Sequence
11	Application
1	CAS Registry Number
42	Cloned(Commentary)
77	Cofactor
1	Crystallization (Commentary)
445	Disease/ Diagnostics
9	Expression
11	General Information
30	IC50 Value
166	Inhibitors
48	kcat/KM [mM/s]
57	Ki Value [mM]
262	KM Value [mM]
40	Localization
1	Metals/Ions
18	Molecular Weight [Da]
93	Natural Substrates/ Products (Substrates)
125	Organism
15	Pathway
4	PDB ID
19	pH Optimum
7	pH Range
2	pH Stability
1	pI Value
73	Protein Variants
25	Purification (Commentary)
6	Reaction
3	Reaction Type
119	Reference
2	Renatured (Commentary)
175	Source Tissue
26	Specific Activity [micromol/min/mg]
2	Storage Stability
299	Substrates and Products (Substrate)
14	Subunits
136	Synonyms
1	Systematic Name
14	Temperature Optimum [°C]
3	Temperature Range [°C]
8	Temperature Stability [°C]
139	Turnover Number [1/s]

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RENATURED/Commentary

ORGANISM

UNIPROT

LITERATURE

between pH 7.4 and 4.5, isoform 3betaHSD2 retains its primarily-helical character with a decrease in alpha-helical content at lower pH values, whereas the beta-sheet content remains unchanged throughout. Titrating the pH back to 7.4 restores the original conformation within 25 min. Metabolic conversion assays indicate peak 3betaHSD2 activity at pH 4.5 with
2fold more progesterone synthesized at pH 4.5 than at pH 3.5 and 7.4. Increasing the 3
betaSD2 concentration from 1 to 40 microg results in a 7fold increase in progesterone at pH 4.5, but no change at pH 7.4. Incubation with guanidinum hydrochloride shows a three-step cooperative unfolding of 3betaHSD2 from pH 7.4 to 4.5, possibly due to the native state unfolding to the intermediate ion core state. With further decreases in pH, increasing concentrations of guanidinum hydrochloride lead to rapid two-step unfolding that may represent complete loss of structure

Homo sapiens

P26439

725511

enzyme interacts strongly with a mixture of dipalmitoylphosphatidylglycerol and dipalmitoylphosphatidylcholine. It becomes less stable when incubated with the individual lipids. Dipalmitoylphosphatidylglycerol, alone or in combination with dipalmitoylphosphatidylcholine, leads to a decrease in alpha-helical content without an effect on the beta-sheet conformation. With the exception of the 20 N-terminal amino acids, mixed vesicles protect the enzyme from trypsin digestion. Protein incubated with dipalmitoylphosphatidylcholine is only partially protected

Homo sapiens

P26439

724302