3.5.4.23: blasticidin-S deaminase

This is an abbreviated version!
For detailed information about blasticidin-S deaminase, go to the full flat file.

Word Map on EC 3.5.4.23

3.5.4.23

license

bipolar

freely

hyperthermia

user

python

open-source

phantom

linux

disinfestation

github

autometallography

hypomanic

deep-seated

strut

molecular biology

biotechnology

Reaction

Synonyms

Bc S deaminase, blasticidin S deaminase, BS deaminase, BSD

ECTree

3 Hydrolases

3.5 Acting on carbon-nitrogen bonds, other than peptide bonds

3.5.4 In cyclic amidines

3.5.4.23 blasticidin-S deaminase

Advanced search results

Do not include text mining results

Include

results (more...)

Include

results (more...)

Results	in table
6	Activating Compound
87	AA Sequence
4	Application
1	CAS Registry Number
19	Cloned(Commentary)
3	Crystallization (Commentary)
2	General Stability
25	Inhibitors
8	KM Value [mM]
3	Metals/Ions
14	Molecular Weight [Da]
32	Natural Substrates/ Products (Substrates)
1	Organic Solvent Stability
40	Organism
26	PDB ID
3	pH Optimum
2	pH Range
3	pH Stability
12	Protein Variants
9	Purification (Commentary)
3	Reaction
3	Reaction Type
37	Reference
2	Renatured (Commentary)
1	Specific Activity [micromol/min/mg]
2	Storage Stability
77	Substrates and Products (Substrate)
9	Subunits
15	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
1	Temperature Range [°C]
3	Temperature Stability [°C]
6	Turnover Number [1/s]

Renatured

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Renatured on EC 3.5.4.23 - blasticidin-S deaminase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide

Go to Renatured Search

reconstitution of the enzyme after denaturation with guanidine-HCl, acid, or p-hydroxymercuriphenylsulfonic acid, using different divalent metal ions, renaturation of the enzyme is completely blocked in presence of 1 mM EDTA, refolding of recombinant Cys91 mutant enzymes from inclusion bodies

Aspergillus terreus

209578

wild-type and deletion mutant apoenzymes, prepared by zinc removal via EDTA, exhibit similar physical properties in thermodynamic refolding into the stable tetramer conformation, reconstitution with zinc

Aspergillus terreus

P0C2P0

654417