2.5.1.48: cystathionine gamma-synthase

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

Reaction

Synonyms

AtCGS, CGS, CGS1, CS,26, cystathionine gamma-synthase, cystathionine synthase, cystathionine synthetase, cystathionine-gamma-synthase, EC 4.2.99.9, homoserine O-transsuccinylase, homoserine transsuccinylase, HTS, MetB, O-succinyl-L-homoserine succinate-lyase (adding cysteine), O-succinylhomoserine (Thiol)-lyase, O-succinylhomoserine synthase, O-succinylhomoserine synthetase, synthase, cystathionine gamma-

ECTree

     2 Transferases

         2.5 Transferring alkyl or aryl groups, other than methyl groups

             2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)

                2.5.1.48 cystathionine gamma-synthase

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
1	Activating Compound
10492	AA Sequence
5	Application
1	CAS Registry Number
20	Cloned(Commentary)
17	Cofactor
9	Crystallization (Commentary)
2	General Information
1	General Stability
4	IC50 Value
41	Inhibitors
40	kcat/KM [mM/s]
14	Ki Value [mM]
76	KM Value [mM]
2	Localization
20	Molecular Weight [Da]
19	Natural Substrates/ Products (Substrates)
93	Organism
10	Pathway
40	PDB ID
10	pH Optimum
2	pH Range
2	Posttranslational Modification
26	Protein Variants
14	Purification (Commentary)
5	Reaction
2	Reaction Type
81	Reference
1	Renatured (Commentary)
21	Source Tissue
14	Specific Activity [micromol/min/mg]
3	Storage Stability
166	Substrates and Products (Substrate)
13	Subunits
34	Synonyms
1	Systematic Name
6	Temperature Optimum [°C]
35	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 2.5.1.48 - cystathionine gamma-synthase

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

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

RENATURED/Commentary

ORGANISM

UNIPROT

LITERATURE

unfolding by guanidinium/HCl inactivates the enzyme due to loss of ketoenamine tautomer. Though pyridoxal 5'-phosphate induces difference in secondary structure content, it is unable to provide stabilizing effect during the overall secondary structure unfolding process. It induces tertiary structure stability of the protein thereby counteracting the deleterious effect of denaturant

Mycobacterium tuberculosis

-

704053