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Literature summary for 2.5.1.48 extracted from

  • Saha, B.; Mukherjee, S.; Das, A.K.
    Molecular characterization of Mycobacterium tuberculosis cystathionine gamma synthase--apo- and holoforms (2009), Int. J. Biol. Macromol., 44, 385-392.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
in silico modeling and pyridoxal 5'-phosphate cofactor docking study Mycobacterium tuberculosis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.32
-
O-succinyl-L-homoserine pH 7.5, 30°C Mycobacterium tuberculosis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
41000
-
4 * 41000, SDS-PAGE Mycobacterium tuberculosis
160000
-
gel filtration, both apo- and holoenzyme Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
-
-

Renatured (Commentary)

Renatured (Comment) Organism
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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
O-succinyl-L-homoserine + H2O gamma-elimination Mycobacterium tuberculosis succinate + 2-oxobutyrate + NH3
-
?

Subunits

Subunits Comment Organism
tetramer 4 * 41000, SDS-PAGE Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate one molecule is attached to one subunit of the protein, apoenzyme is completely inactive. 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