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Authors: Ballou DP | Entsch B
Date: 2013
Subject: Enzymes
Language: en
Type of item: book chapter
Identifier: vtls086673514
Description: Flavoprotein monooxygenases, found in species ranging from microorganisms to mammals, transfer one oxygen atom derived from O₂ to a substrate, oxidizing it. In this chapter, we review the enzymes in G ... show more
Date: 2010
Subject: Enzymes
Language: en
Type of item: journal article
Identifier: une-20100122-154816
Description: There are two known types of microbial two-component flavin-dependent monooxygenases that catalyze oxygenation of p-hydroxyphenylacetate (HPA), and they are distinguished by having structurally distin ... show more
Refereed: Refereed
Authors: Entsch B | Ballou DP
Date: 2009
Language: en
Type of item: entry in reference work
Identifier: pes:7004
Description: Flavins react with oxygen and can form stable flavin peroxides in an aprotic solvent or buried in a protein. It is this hydroperoxide or peroxide that is the oxygenating agent in flavoproteins. This p ... show more
Date: 2008
Subject: Bacteriology
Language: en
Type of item: journal article
Identifier: pes:5955
Description: The 'luxG' gene is part of the 'lux' operon of marine luminous bacteria. 'luxG' has been proposed to be a flavin reductase that supplies reduced flavin mononucleotide (FMN) for bacterial luminescence. ... show more
Refereed: Refereed
Date: 2007
Subject: Enzymes
Language: en
Type of item: journal article
Identifier: pes:4976
Description: p-Hydroxyphenylacetate hydroxylase (HPAH) from 'Acinetobacter baumannii' catalyzes the hydroxylation of p-hydroxyphenylacetate (HPA) to form 3,4-dihydroxyphenylacetate (DHPA). HPAH is composed of two ... show more
Refereed: Refereed
Date: 2007
Subject: Enzymes
Language: en
Type of item: journal article
Identifier: pes:5956
Description: A new luciferase from 'V. campbellii' (Lux_Vc) was cloned and expressed in Escherichia coli and purified to homogeneity. Although the amino acid sequences and the catalytic reactions of Lux_Vc are hig ... show more
Refereed: Refereed
Date: 2006
Subject: Enzymes
Language: en
Type of item: journal article
Identifier: une-20130822-163043
Description: p-Hydroxyphenylacetate hydroxylase (HPAH) from 'Acinetobacter baumannii' catalyzes the hydroxylation of p-hydroxyphenylacetate (HPA) to form 3,4-dihydroxyphenylacetate (DHPA).The enzyme system is comp ... show more
Refereed: Refereed
Date: 2005
Language: en
Type of item: journal article
Identifier: une-20130822-161441
Description: ρ-Hydroxybenzoate hydroxylase (PHBH) is a homodimeric enzyme in which each subunit noncovalently binds one molecule of FAD in the active site. PHBH is a model system for how flavoenzymes regulate reac ... show more
Refereed: Refereed
Authors: Ballou DP | Entsch B | Cole LJ
Date: 2005
Subject: Enzymes
Language: en
Type of item: journal article
Identifier: une-20130822-174655
Description: Flavoprotein monooxygenases are involved in a wide variety of biological processes including drug detoxification, biodegradation of aromatic compounds in the environment, biosynthesis of antibiotics a ... show more
Refereed: Refereed
Date: 2005
Subject: Enzymes
Language: en
Type of item: journal article
Identifier: pes:3889
Description: p-Hydroxybenzoate hydroxylase is extensively studied as a model for single-component flavoprotein monooxygenases. It catalyzes a reaction in two parts:  (1) reduction of the FAD in the enzyme by NADPH ... show more
Refereed: Refereed
Authors: Entsch B | Cole LJ | Ballou DP
Date: 2005
Subject: Enzymes
Language: en
Type of item: journal article
Identifier: une-20130822-164645
Description: 'para'-Hydroxybenzoate hydroxylase is a flavoprotein monooxygenase that catalyzes a reaction in two parts: reduction of the enzyme cofactor, FAD, by NADPH in response to binding 'p'-hydroxybenzoate to ... show more
Refereed: Refereed
Date: 2005
Subject: Enzymes
Language: en
Type of item: journal article
Identifier: une-20130819-162740
Description: ρ-Hydroxybenzoate hydroxylase (PHBH) is a homodimeric flavoprotein monooxygenase that catalyzes the hydroxylation of ρ-hydroxybenzoate to form 3,4-dihydroxybenzoate. Controlled catalysis is achieved b ... show more
Refereed: Refereed
Date: 2005
Subject: Enzymes
Language: en
Type of item: journal article
Identifier: une-20130821-161218
Description: p-Hydroxyphenylacetate (HPA) hydroxylase (HPAH) from 'Acinetobacter baumannii' catalyzes hydroxylation of HPA to form 3,4-dihydroxyphenylacetate. It is a two protein system consisting of a smaller red ... show more
Refereed: Refereed
Date: 2004
Subject: Enzymes
Language: en
Type of item: journal article
Identifier: une-20130819-151416
Description: Para-hydroxybenzoate hydroxylase is a flavoprotein monooxygenase that catalyzes a reaction in two parts: reduction of the enzyme cofactor, FAD, by NADPH in response to binding ρ-hydroxybenzoate to the ... show more
Refereed: Refereed
Date: 2004
Subject: Enzymes
Language: en
Type of item: journal article
Identifier: une-20130819-16155
Description: 'para'-Hydroxybenzoate hydroxylase is a flavoprotein monooxygenase that catalyses a reaction in two parts: reduction of the flavin adenine dinucleotide (FAD) in the enzyme by reduced nicotinamide aden ... show more
Refereed: Refereed