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Literature summary extracted from

  • Campanini, B.; Schiaretti, F.; Abbruzzetti, S.; Kessler, D.; Mozzarelli, A.
    Sulfur mobilization in cyanobacteria: the catalytic mechanism of L-cystine C-S lyase (C-DES) from synechocystis (2006), J. Biol. Chem., 281, 38769-38780.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.4.1.13
-
 Synechocystis sp. PCC 6714

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.4.1.13
-
 Synechocystis sp. PCC 6714

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.4.1.13 1
-
 cystine estimated from steady-state measurements Synechocystis sp. PCC 6714

Organism

EC Number Organism UniProt Comment Textmining
4.4.1.13 Synechocystis sp. PCC 6714
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.4.1.13
-
 Synechocystis sp. PCC 6714

Storage Stability

EC Number Storage Stability Organism
4.4.1.13 -80°C, 10 mM MOPS buffer, pH 6.5 Synechocystis sp. PCC 6714

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.4.1.13 L-cystine + H2O
-
 Synechocystis sp. PCC 6714 L-thiocysteine + pyruvate + NH3
-
 ?
4.4.1.13 L-cystine + H2O cystine is preferred over cysteine as substrate Synechocystis sp. PCC 6714 L-thiocysteine + pyruvate + NH3
-
 ?

Subunits

EC Number Subunits Comment Organism
4.4.1.13 homodimer
-
 Synechocystis sp. PCC 6714

Synonyms

EC Number Synonyms Comment Organism
4.4.1.13 L-cystine C-S lyase
-
 Synechocystis sp. PCC 6714

Cofactor

EC Number Cofactor Comment Organism Structure
4.4.1.13 pyridoxal 5'-phosphate bound by Lys-223 in the active site Synechocystis sp. PCC 6714