NDLI: Hydroxylation by flavin enzymes : evidence for NIH-shift mechanism

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Hydroxylation by flavin enzymes : evidence for NIH-shift mechanism

Content Provider	Semantic Scholar
Author	Eisenreich, Wolfgang Hultschig, Claus Hartmann, Steffen Fuchs, Georg Bacher, Adelbert Ghisla, Sandro
Copyright Year	1999
Abstract	2-Aminobenzoate is an intermediate in many catabolic pathways. More specificaIly, biodegradation oftryptophan, indole acetic acid, and indole alkaloids yields 2aminobenzoate as a common intermediate. Under aerobic conditions 2aminobenzoate is further degraded via gentisate or catechol [1]. Rather recently, a novel pathway of2-aminobenzoate metabolism has been elucidated. It has been shown in the eubacterium Azoarcus evansii that 2aminobenzoate and coenzyme Aare converted into 2-aminobenzoyl CoA by the catalytic action of a specific ligase [2]. 2-Aminobenzoyl CoA can then serve as substrate of a monoxygenase/reductase [3-6]. More specifically, the flavoprotein 2aminobenzoyl CoA monooxygenase/reductase (ACMR) catalyzes the dearomatization of2-aminobenzoyl CoA in a NADHand Oz-dependent reaction by a hitherto unknown mechanism. The enzyme is a dimer comprising two 85 kDa polypeptide chains and contains one FAO per subunit. Based on earlier studies, ACMR contains two domains (a monooxygenase and a reductase site) each containing one FAO molecule [3-5]. In this study, the structure of the enzyme product and the mechanism of its formation are analyzed by NMR spectroscopy. .."
Starting Page	359
Ending Page	366
Page Count	8
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://kops.uni-konstanz.de/bitstream/handle/123456789/6710/Hydroxylation_by_flavin_enzymes.pdf?isAllowed=y&sequence=1
Alternate Webpage(s)	https://kops.uni-konstanz.de/bitstream/handle/123456789/6710/Hydroxylation_by_flavin_enzymes.pdf?isAllowed=y&sequence=1
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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