Literature summary for 1.14.13.128 extracted from

Retnadhas, S.; Gummadi, S.N.
Identification and characterization of oxidoreductase component (NdmD) of methylxanthine oxygenase system in Pseudomonas sp. NCIM 5235 (2018), Appl. Microbiol. Biotechnol., 102, 7913-7926 .

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Cloned(Commentary)

Cloned (Comment)	Organism
gene ndmC, genetic organization of caffeine-degrading genes and its isolation	Pseudomonas sp. NCIM 5235

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
7-methylxanthine + O2 + NAD(P)H + H+	Pseudomonas sp. NCIM 5235	-	xanthine + NAD(P)+ + H2O + formaldehyde	-	?

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas sp. NCIM 5235	A0A2U9IY60	isolated from coffee plantation soil in Ooty, India	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
cell culture	strain NCIM 5235 can utilize caffeine as sole source of carbon and nitrogen for growth	Pseudomonas sp. NCIM 5235	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
7-methylxanthine + O2 + NAD(P)H + H+	-	Pseudomonas sp. NCIM 5235	xanthine + NAD(P)+ + H2O + formaldehyde	-	?

Subunits

Subunits	Comment	Organism
More	NdmC forms a large multi-subunit complex comprising 2 monomeric units of each NdmC, NdmD, and NdmE and follows the typical electron flow pattern of Rieske oxygenases. The Rieske domain present in NdmD serves to function as an electron transfer domain during catalysis by NdmC as it lacks its own Rieske domain	Pseudomonas sp. NCIM 5235

Synonyms

Synonyms	Comment	Organism
NdmC	-	Pseudomonas sp. NCIM 5235

Cofactor

Cofactor	Comment	Organism	Structure
NAD(P)H	-	Pseudomonas sp. NCIM 5235

General Information

General Information	Comment	Organism
evolution	the N-terminal Rieske domain found in NdmD is a product of domain shuffling between NdmC and NdmD during evolution and is not required for its reductase activity	Pseudomonas sp. NCIM 5235
additional information	based on the sequence of a genomic fragment, caffeine demethylation enzyme system found in Pseudomonas sp. is predicted to consist of a two-component Rieske monooxygenases namely NdmA and NdmB specific towards methyl groups at 1 and 3 positions in xanthine ring respectively and one kind of three-component Rieske monooxygenase system comprising a monooxygenase NdmC specific towards 7-methylxanthine, a reductase component NdmD and a structural protein NdmE. NdmD also acts as the reductase component for NdmA and NdmB. The Rieske domain present in NdmD serves to function as an electron transfer domain during catalysis by NdmC as it lacks its own Rieske domain. NdmC forms a large multi-subunit complex comprising 2 monomeric units of each NdmC, NdmD, and NdmE and follows the typical electron flow pattern of Rieske oxygenases. The N-terminal Rieske domain found in NdmD is a product of domain shuffling between NdmC and NdmD during evolution and is not required for its reductase activity	Pseudomonas sp. NCIM 5235
physiological function	Pseudomonas sp. NCIM 5235 is a caffeine-degrading bacterial strain that metabolizes caffeine by sequential demethylation using methylxanthine demethylases, including 7-methylxanthine demethylase NdmC. These enzymes belong to the class of two-component Rieske oxygenases and require an oxidoreductase, NdmD, for efficient catalysis. Three oxygenases (NdmA, NdmB, and NdmC) specific towards methyl groups at 1, 3, and 7 positions in xanthine ring share a common reductase component, NdmD, analysis of NdmD parameters and function, overview. Another structural protein and oxidoreductase NdmE has also been shown to be required for catalysis by NdmC. Rieske oxygenases are an important class of enzymes that have been reported to play a major role in the degradation of xenobiotic compounds and drugs	Pseudomonas sp. NCIM 5235

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Release 2023.1 (January 2023)