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3,4-dihydroxyphenylacetate 2,3-dioxygenase

Known as: 3,4-DHPA 2,3-dioxygenase, homoprotocatechuate 2,3-dioxygenase 
 
National Institutes of Health

Papers overview

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Review
2014
Review
2014
Extradiol-cleaving catechol dioxygenases function by binding both the organic substrate and O2 at a divalent metal center in the… Expand
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2012
2012
Homoprotocatechuate 2,3-dioxygenase (FeHPCD) utilizes an active site Fe(II) to activate O(2) in a reaction cycle that ultimately… Expand
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2011
2011
Substrates homoprotocatechuate (HPCA) and O(2) bind to the Fe(II) of homoprotocatechuate 2,3-dioxygenase (FeHPCD) in adjacent… Expand
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Highly Cited
2008
Highly Cited
2008
The reactive oxy intermediate of the catalytic cycle of extradiol aromatic ring-cleaving dioxygenases is formed by binding the… Expand
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Highly Cited
2005
Highly Cited
2005
Homoprotocatechuate 2,3-dioxygenase (WT 2,3-HPCD) isolated from Brevibacterium fuscum utilizes an active site Fe(II) and O(2) to… Expand
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2005
2005
The manganese-dependent 3,4-dihydroxyphenylacetate 2,3-dioxygenase (MndD) from Arthrobacter globiformis CM-2 is an extradiol… Expand
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Highly Cited
2004
Highly Cited
2004
The X-ray crystal structures of homoprotocatechuate 2,3-dioxygenases isolated from Arthrobacter globiformis and Brevibacterium… Expand
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Highly Cited
2004
Highly Cited
2004
Homoprotocatechuate 2,3-dioxygenase isolated from Brevibacterium fuscum utilizes an active site Fe(II) and O(2) to catalyze… Expand
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2003
2003
The intra- and extradiol subfamilies of catechol-adduct ring-cleaving dioxygenases each exhibit nearly absolute fidelity for the… Expand
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Highly Cited
1996
Highly Cited
1996
Homoprotocatechuate 2,3-dioxygenase (2,3-HPCD) cleaves the aromatic ring of its substrate with insertion of both atoms of oxygen… Expand
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