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

BRENDA support

Literature summary extracted from

  • Song, H.; Her, A.; Raso, F.; Zhen, Z.; Huo, Y.; Liu, P.
    Cysteine oxidation reactions catalyzed by a mononuclear non-heme iron enzyme (OvoA) in ovothiol biosynthesis (2014), Org. Lett., 16, 2122-2125 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.14.99.52 E176H site-directed mutagenesis, the mutation changes OvoA from a 2-His-1-carboxylate to a 3-His ligand environment if the new third histidine residue replaces glutamate as the metal ligand. The mutant enzyme not only loses the cysteine dioxygenase activity but also stops catalyzing the formation of oxidative coupling products S-(L-histidin-5-yl)-L-cysteine S-oxide and cysteine sulfinic acid. The 2-His-1-carboxylate catalytic triad disrupts the cysteine dioxygenase activity Erwinia tasmaniensis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.99.52 Fe2+ a mononuclear non-heme iron enzyme Erwinia tasmaniensis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.99.52 hercynine + L-cysteine + O2 Erwinia tasmaniensis reaction of EC 1.14.99.51 S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
 ?
1.14.99.52 L-histidine + L-cysteine + O2 Erwinia tasmaniensis
-
 S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
 ?
1.14.99.52 additional information Erwinia tasmaniensis OvoA in ovothiol biosynthesis is a mononuclear non-heme iron enzyme catalyzing the oxidative coupling between L-histidine and L-cysteine. It can also catalyze the oxidative coupling between hercynine and cysteine, yet with a different regioselectivity (cf. Ec 1.14.99.51). OvoA can also catalyze the oxidation of cysteine to either cysteine sulfinic acid or cystine, OvoA has cysteine dioxygenase activity (cf. EC 1.13.11.20). A 3-His catalytic triad is a prerequisite for the cysteine dioxygenase activity ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.99.52 Erwinia tasmaniensis
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.99.52 hercynine + L-cysteine + O2 reaction of EC 1.14.99.51 Erwinia tasmaniensis S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
 ?
1.14.99.52 L-histidine + L-cysteine + O2
-
 Erwinia tasmaniensis S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
 ?
1.14.99.52 additional information OvoA in ovothiol biosynthesis is a mononuclear non-heme iron enzyme catalyzing the oxidative coupling between L-histidine and L-cysteine. It can also catalyze the oxidative coupling between hercynine and cysteine, yet with a different regioselectivity (cf. Ec 1.14.99.51). OvoA can also catalyze the oxidation of cysteine to either cysteine sulfinic acid or cystine, OvoA has cysteine dioxygenase activity (cf. EC 1.13.11.20). A 3-His catalytic triad is a prerequisite for the cysteine dioxygenase activity Erwinia tasmaniensis ?
-
 ?
1.14.99.52 additional information the OvoA-catalyzed reactions can be systematically modulated by a slight modification of one of its substrates, L-histidine. Substrate specificity of OvoA, detailed overview Erwinia tasmaniensis ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.99.52 OvoA
-
 Erwinia tasmaniensis

General Information

EC Number General Information Comment Organism
1.14.99.52 metabolism OvoA in ovothiol biosynthesis catalyzes the oxidative coupling between L-histidine and L-cysteine. It can also catalyze the oxidative coupling between hercynine and cysteine, yet with a different regioselectivity. OvoA can also catalyze the oxidation of cysteine to either cysteine sulfinic acid or cystine. Formation of S-(L-histidin-5-yl)-L-cysteine S-oxide and cysteine sulfinic acid might be two branching pathways in OvoA catalysis Erwinia tasmaniensis
1.14.99.52 additional information structure modeling and sequence comparisons Erwinia tasmaniensis