Re-face stereospecificity of NADP dependent methylenetetrahydromethanopterin dehydrogenase from Methylobacterium extorquens AM1 as determined by NMR spectroscopy.

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Generation of formate by the formyltransferase/hydrolase complex (Fhc) from Methylobacterium extorquens AM1.Methylotrophy in Methylobacterium extorquens AM1 from a genomic point of view.

P2860

Q34139515-0A8261B4-0E5E-4894-B5F3-38B93F866D7F Q35120956-540EC630-51AB-459E-B5FF-E265B9EBE840

P2860

Re-face stereospecificity of NADP dependent methylenetetrahydromethanopterin dehydrogenase from Methylobacterium extorquens AM1 as determined by NMR spectroscopy.

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http://www.wikidata.org/entity/Q43571738

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2001 nî lūn-bûn

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2001年の論文

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2001年学术文章

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2001年学术文章

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2001年学术文章

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2001年学术文章

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2001年学术文章

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2001年学术文章

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2001年學術文章

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2001年學術文章

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name

Re-face stereospecificity of N ...... etermined by NMR spectroscopy.

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Re-face stereospecificity of N ...... etermined by NMR spectroscopy.

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type

Item

label

Re-face stereospecificity of N ...... etermined by NMR spectroscopy.

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Re-face stereospecificity of N ...... etermined by NMR spectroscopy.

@nl

prefLabel

Re-face stereospecificity of N ...... etermined by NMR spectroscopy.

@en

Re-face stereospecificity of N ...... etermined by NMR spectroscopy.

@nl

P1476

Re-face stereospecificity of N ...... determined by NMR spectroscopy

@en

P2093

C Griesinger

http://www.w3.org/2001/XMLSchema#string

C H Hagemeier

http://www.w3.org/2001/XMLSchema#string

R K Thauer

http://www.w3.org/2001/XMLSchema#string

S Bartoschek

http://www.w3.org/2001/XMLSchema#string

P2860

The crystal structure of a bacterial, bifunctional 5, 10 methylene-tetrahydrofolate dehydrogenase/cyclohydrolase

The 3-D structure of a folate-dependent dehydrogenase/cyclohydrolase bifunctional enzyme at 1.5 A resolution

Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy

Phylogenetic analysis of 18 thermophilic Methanobacterium isolates supports the proposals to create a new genus, Methanothermobacter gen. nov., and to reclassify several isolates in three species, Methanothermobacter thermautotrophicus comb. nov., M

Tetrahydrofolate and tetrahydromethanopterin compared: functionally distinct carriers in C1 metabolism

H2-forming N5, N10-methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautotrophicum catalyzes a stereoselective hydride transfer as determined by two-dimensional NMR spectroscopy.

Salt dependence, kinetic properties and catalytic mechanism of N-formylmethanofuran:tetrahydromethanopterin formyltransferase from the extreme thermophile Methanopyrus kandleri.

H2-forming methylenetetrahydromethanopterin dehydrogenase, a novel type of hydrogenase without iron-sulfur clusters in methanogenic archaea.

Substrate flux through methylenetetrahydrofolate dehydrogenase: predicted effects of the concentration of methylenetetrahydrofolate on its partitioning into pathways leading to nucleotide biosynthesis or methionine regeneration.

Characterization of a second methylene tetrahydromethanopterin dehydrogenase from Methylobacterium extorquens AM1

P304

95-98

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scholarly article

P356

10.1016/S0014-5793(01)02306-7

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English

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1-2

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494

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Julia Vorholt

P577

2001-04-01T00:00:00Z

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P698

11297742

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Re-face stereospecificity of NADP dependent methylenetetrahydromethanopterin dehydrogenase from Methylobacterium extorquens AM1 as determined by NMR spectroscopy.

about

P2860

P2860

Re-face stereospecificity of NADP dependent methylenetetrahydromethanopterin dehydrogenase from Methylobacterium extorquens AM1 as determined by NMR spectroscopy.

description

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P698