4.4.1.9: L-3-cyanoalanine synthase

This is an abbreviated version!
For detailed information about L-3-cyanoalanine synthase, go to the full flat file.

Reaction

Synonyms

AtcysC1, beta-CAS, beta-cyano-L-alanine synthase, beta-cyanoalanine synthase, beta-cyanoalanine synthetase, BsaS, Bsas3, BsasA, BsasB, CAS, CAS1, CAS2, cyanoalanine synthase, CYS-C1, L-cysteine hydrogen-sulfide-lyase, L-cysteine: hydrogen sulphide lyase, O-acetyl-L-serine sulfhydrylase, PCAS-1, PCAS-2, synthase,.beta.-cyanoalanine, Tu-CAS

ECTree

     4 Lyases

         4.4 Carbon-sulfur lyases

             4.4.1 Carbon-sulfur lyases (only sub-subclass identified to date)

                4.4.1.9 L-3-cyanoalanine synthase

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
18	Activating Compound
50	AA Sequence
3	Application
1	CAS Registry Number
12	Cloned(Commentary)
18	Cofactor
1	Crystallization (Commentary)
11	General Information
2	IC50 Value
40	Inhibitors
2	kcat/KM [mM/s]
16	Ki Value [mM]
89	KM Value [mM]
22	Localization
3	Metals/Ions
25	Molecular Weight [Da]
35	Natural Substrates/ Products (Substrates)
82	Organism
5	Pathway
22	pH Optimum
6	pH Range
1	pH Stability
1	pI Value
1	Protein Variants
24	Purification (Commentary)
2	Reaction
2	Reaction Type
78	Reference
68	Source Tissue
36	Specific Activity [micromol/min/mg]
3	Storage Stability
120	Substrates and Products (Substrate)
15	Subunits
48	Synonyms
1	Systematic Name
6	Temperature Optimum [°C]
1	Temperature Range [°C]
3	Temperature Stability [°C]
14	Turnover Number [1/s]

Crystallization

print visible entries

print all entries

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

Crystallization on EC 4.4.1.9 - L-3-cyanoalanine synthase

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

top print hide Go to Crystallization (commentary) Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

purified recombinant wild-type and K95A mutant enzymes, hanging drops vapor diffusion method , 0004 ml of 10-12 mg/ml protein solution is mixed with an equal volume of crystallization solution containing 10% PEG 8000, 0.2 M NaCl, and 0.1 sodium/potassium phosphate, pH 7.0, and 0.2 M MgSO4, at 4°C over a 0.7 mL reservoir. The K95A mutant is crystallized in similar drops from a solution containing 20% PEG 3350, 0.2 M potassium citrate, pH 7.5, X-ray diffraction structure determination and analysis at 2.50 A and 1.77 A resolution, respectively, molecular replacement

Glycine max

I1L6I6

730601