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

BRENDA support

Refine search

Search General Information

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search

Search term:

Results 1 - 10 of 11 > >>
EC Number
General Information
Commentary
Reference
evolution
emzyme PsEFE should be regarded as a hybrid of subgroups I and II, in terms of its classification
evolution
enzyme EFE is a member of the mononuclear non-heme Fe(II)- and 2-oxoglutarate (2OG)-dependent oxygenase superfamily. It contains a double-stranded beta-helix (DSBH, also known as the jellyroll or cupin fold) core typically found in members of the Fe(II)/2OG-dependent oxygenases
evolution
ethylene-forming enzyme (EFE) is a member of the mononuclear non-heme Fe(II)- and 2-oxoglutarate (2OG)-dependent oxygenase superfamily
evolution
the enzyme belongs to a subclass of 2-oxoglutarate/Fe(II) dependent dioxygenases, structure-function analysis of the ethylene forming subclass of 2-oxoglutarate/Fe(II)-dependent dioxygenases, overview
evolution
the enzyme belongs to a subclass of 2-oxoglutarate/Fe(II) dependent dioxygenases, structure-function analysis of the ethylene forming subclass of 2-oxoglutarate/Fe(II)-dependent dioxygenases,overview
metabolism
analysis enzyme EFE reaction and cellular carbon flux, overview
more
three of the amino acids correlating with ethylene production are located in the predicted 2-oxoglutarate binding domain, a protein domain specific for the EFE-class that is essential for activity. Residues H189, D191 and H268 are responsible for binding the Fe(II) ligand
physiological function
a non-heme Fe(II)- and 2-oxoglutarate-dependent ethylene-forming enzyme, EFE converts 2-oxoglutarate into ethylene plus three CO2 molecules while also catalyzing the C5 hydroxylation of L-arginine driven by the oxidative decarboxylation of 2-oxoglutarate to form succinate and CO2
physiological function
in the presence of O2, the enzyme catalyzes ethylene formation from the substrates 2-oxoglutarate and L-arginine
physiological function
the enzyme is reported to simultaneously catalyze the conversion of 2OG into ethylene plus three CO2 and the Cdelta hydroxylation of L-arginine (L-Arg) while oxidatively decarboxylating 2OG to form succinate and carbon dioxide. The enzyme produces ethylene, a gas that is widely used as a building block in the production of various plastics, detergents, surfactants, antifreeze, solvents, and other important industrial materials. And ethylene is a plant hormone that plays an important role in growth and development. The ethylene-forming reaction is not intrinsically linked to L-Arg hydroxylation
Results 1 - 10 of 11 > >>