Dioxygenase

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
<StructureSection load='1eob' size='350' side='right' caption='Structure of protocatechuate 3,4-dioxygenase with Fe+3 complex with dihydroxybenzoate (PDB entry [[1eob]])' scene=''>
<StructureSection load='1eob' size='350' side='right' caption='Structure of protocatechuate 3,4-dioxygenase with Fe+3 complex with dihydroxybenzoate (PDB entry [[1eob]])' scene=''>
-
'''Dioxygenases''' cleave the aromatic rings of their substrates by inserting two oxygen atoms, thus degrading these compounds. The dioxygenases are divided into 2 groups according to their mode of ring scission. The intradiol enzymes use Fe+3 as cofactor and cleave the substrate between 2 hydroxyl groups. The extradiol enzymes use Fe+2 as cofactor and cleave the substrate between a hydroxylated carbon and a non-hydroxylated one. '''Protocatechuate 3,4-dioxygenase''' (PCD), belongs to the intradiol family and catalyzes the oxygenation of dihydroxybenzoate (DHB) to 3-carboxy-muconate. PCD participates in the aromatic compound benzoate degredation and uses Fe as cofactor. PCD consists of 8 subunits each containing an Fe and a substrate binding site. Each of these subunits is composed of α and β chains. Hydroxyphenyl acetate is an inhibitor of PCD. '''Catechol 1,2-dioxygenase''' (CTD) cleaves the ring of catechol by insertion of 2 oxygen atoms to form muconic acid. '''Homoprotocatechuate 3,4-dioxygenase''' (HPCD), an extradiol cleaving enzyme cleaves the aromatic ring of its substrate, adds 2 oxygen atoms to form α-hydroxy-δ carboxymethyl muconic semialdehyde. '''Naphthalene 1,2-dioxygenase''' (NDO) catalyzes the conversion of naphthalene and O2 to dihydronaphthalene-diol.
+
'''Dioxygenases''' cleave the aromatic rings of their substrates by inserting two oxygen atoms, thus degrading these compounds. The dioxygenases are divided into 2 groups according to their mode of ring scission. The intradiol enzymes use Fe+3 as cofactor and cleave the substrate between 2 hydroxyl groups. The extradiol enzymes use Fe+2 as cofactor and cleave the substrate between a hydroxylated carbon and a non-hydroxylated one. <br />
 +
* '''Protocatechuate 3,4-dioxygenase''' (PCD), belongs to the intradiol family and catalyzes the oxygenation of dihydroxybenzoate (DHB) to 3-carboxy-muconate. PCD participates in the aromatic compound benzoate degredation and uses Fe as cofactor. PCD consists of 8 subunits each containing an Fe and a substrate binding site. Each of these subunits is composed of α and β chains. Hydroxyphenyl acetate is an inhibitor of PCD.<br />
 +
* '''Catechol 1,2-dioxygenase''' (CTD) cleaves the ring of catechol by insertion of 2 oxygen atoms to form muconic acid.<br />
 +
* '''Homoprotocatechuate 3,4-dioxygenase''' (HPCD), an extradiol cleaving enzyme cleaves the aromatic ring of its substrate, adds 2 oxygen atoms to form α-hydroxy-δ carboxymethyl muconic semialdehyde.<br />
 +
* '''Naphthalene 1,2-dioxygenase''' (NDO) catalyzes the conversion of naphthalene and O2 to dihydronaphthalene-diol.
==3D structures of Protocatechuate 3,4-dioxygenase==
==3D structures of Protocatechuate 3,4-dioxygenase==

Revision as of 10:39, 17 August 2014

Structure of protocatechuate 3,4-dioxygenase with Fe+3 complex with dihydroxybenzoate (PDB entry 1eob)

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman, Jaime Prilusky

Personal tools