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Literature summary for 4.4.1.1 extracted from

  • Araki, S.; Takata, T.; Ono, K.; Sawa, T.; Kasamatsu, S.; Ihara, H.; Kumagai, Y.; Akaike, T.; Watanabe, Y.; Tsuchiya, Y.
    Cystathionine gamma-lyase self-inactivates by polysulfidation during cystine metabolism (2023), Int. J. Mol. Sci., 24, 9982.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli DH5alpha cells Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
C136V the mutant with increased beta-lyase activity toward L-cystine compared to the wild type enzyme is not inhibited by cysteine persulfide or Na2S4 Rattus norvegicus
C136V/C171V the mutant shows increased beta-lyase activity toward L-cystine and reduced gamma-lyase activity toward cystathionine compared to the wild type enzyme. The mutant is not inhibited by cysteine persulfide or Na2S4. The cysteine persulfide-producing activity of the mutant is higher than that of the wild type enzyme. Meanwhile, the cysteine-producing activity of this mutant is equivalent to that of the wild type enzyme Rattus norvegicus
C171V the mutant with wild type activity is inhibited by cysteine persulfide or Na2S4 Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
cysteine persulfide
-
Rattus norvegicus
Na2S2 pretreatment of immobilized enzyme with Na2S2 causes the inhibition of its beta-lyase activity toward L-cystine Rattus norvegicus
Na2S3 pretreatment of immobilized enzyme with Na2S3 causes the inhibition of its beta-lyase activity toward L-cystine Rattus norvegicus
Na2S4 pretreatment of immobilized enzyme with 0.01 mM Na2S4 causes the inhibition of its beta-lyase activity toward L-cystine, which is completely recovered by the addition of dithiothreitol or Tris-(2-carboxyethyl)phosphine Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.271
-
L-cystine wild type enzyme, at pH 7.5 and 37°C Rattus norvegicus
0.308
-
L-cystine mutant enzyme C171V, at pH 7.5 and 37°C Rattus norvegicus
0.32
-
L-cystine mutant enzyme C136V/C171V, at pH 7.5 and 37°C Rattus norvegicus
0.554
-
L-cystine mutant enzyme C136V, at pH 7.5 and 37°C Rattus norvegicus
6.13
-
beta-chloro-L-alanine mutant enzyme C171V, at pH 8.0 and 37°C Rattus norvegicus
7.57
-
beta-chloro-L-alanine wild type enzyme, at pH 8.0 and 37°C Rattus norvegicus
8.4
-
beta-chloro-L-alanine mutant enzyme C136V/C171V, at pH 8.0 and 37°C Rattus norvegicus
11.77
-
beta-chloro-L-alanine mutant enzyme C136V, at pH 8.0 and 37°C Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-cystathionine + H2O Rattus norvegicus
-
L-cysteine + 2-oxobutanoate + NH3
-
?
L-cystine + H2O Rattus norvegicus
-
cysteine persulfide + pyruvate + NH3
-
?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information enzyme polysulfidation occurs at Cys136 during cystine metabolism and functions to down-regulate cysteine persulfide synthesis by the enzyme Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-chloro-L-alanine + H2O
-
Rattus norvegicus pyruvate + NH3 + HCl
-
?
L-cystathionine + H2O
-
Rattus norvegicus L-cysteine + 2-oxobutanoate + NH3
-
?
L-cystine + H2O
-
Rattus norvegicus cysteine persulfide + pyruvate + NH3
-
?

Subunits

Subunits Comment Organism
? x * 45000, SDS-PAGE Rattus norvegicus

Synonyms

Synonyms Comment Organism
CSE
-
Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
Rattus norvegicus

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.005
-
wild type enzyme, at pH 7.5 and 30°C Rattus norvegicus Na2S4
0.007
-
wild type enzyme, at pH 7.5 and 30°C Rattus norvegicus Na2S3
0.02
-
wild type enzyme, at pH 7.5 and 30°C Rattus norvegicus Na2S2