Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Salsi, E.; Campanini, B.; Bettati, S.; Raboni, S.; Roderick, S.L.; Cook, P.F.; Mozzarelli, A.
    A two-step process controls the formation of the bienzyme cysteine synthase complex (2010), J. Biol. Chem., 285, 12813-12822.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.47 expressed in Escherichia coli Haemophilus influenzae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.47 additional information Haemophilus influenzae stopped-flow fluorescence spectroscopy is used to characterize the interaction of serine acetyltransferase with OASS and in the presence of the physiological regulators cysteine and bisulfide. Cysteine synthase assembly occurs via a two-step mechanism involving rapid formation of an encounter complex between the two enzymes, followed by a slow conformational change. The conformational change likely results from the closure of the active site of OASS upon binding of the serine acetyltransferase C-terminal peptide. Bisulfide stabilizes the cysteine synthase complex mainly by decreasing the back rate of the isomerization step. Cysteine, the product of the OASS reaction and a SAT inhibitor, slightly affects the kinetics of cysteine synthase formation leading to destabilization of the complex ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.47 Haemophilus influenzae
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.47 additional information stopped-flow fluorescence spectroscopy is used to characterize the interaction of serine acetyltransferase with OASS and in the presence of the physiological regulators cysteine and bisulfide. Cysteine synthase assembly occurs via a two-step mechanism involving rapid formation of an encounter complex between the two enzymes, followed by a slow conformational change. The conformational change likely results from the closure of the active site of OASS upon binding of the serine acetyltransferase C-terminal peptide. Bisulfide stabilizes the cysteine synthase complex mainly by decreasing the back rate of the isomerization step. Cysteine, the product of the OASS reaction and a SAT inhibitor, slightly affects the kinetics of cysteine synthase formation leading to destabilization of the complex Haemophilus influenzae ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.5.1.47 O-acetylserine sulfhydrylase cysteine synthase is a multiprotein assembly formed by the pyridoxal 5'-phosphate-dependent enzyme O-acetylserine sulfhydrylase and serine acetyltransferase Haemophilus influenzae
2.5.1.47 OASS
-
 Haemophilus influenzae