Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme. - sprookjes - yvandenbroek - TriplyDB

Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme.

Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme.

http://www.wikidata.org/entity/Q36107587

about

New insights into the reductive half-reaction mechanism of aromatic amine dehydrogenase revealed by reaction with carbinolamine substrates New pathway of amine oxidation respiratory chain of Paracoccus denitrificans IFO 12442.Gated and ungated electron transfer reactions from aromatic amine dehydrogenase to azurin.Intrigues and intricacies of the biosynthetic pathways for the enzymatic quinocofactors: PQQ, TTQ, CTQ, TPQ, and LTQ Cupredoxins--a study of how proteins may evolve to use metals for bioenergetic processes.Heterologous expression of correctly assembled methylamine dehydrogenase in Rhodobacter sphaeroides.Localization of periplasmic redox proteins of Alcaligenes faecalis by a modified general method for fractionating gram-negative bacteria.The structure and function of methanol dehydrogenase and related quinoproteins containing pyrrolo-quinoline quinone.Quinoprotein-catalysed reactions.Kinetic and chemical mechanisms for the effects of univalent cations on the spectral properties of aromatic amine dehydrogenase Barrier compression and its contribution to both classical and quantum mechanical aspects of enzyme catalysis.Identification of reaction products and intermediates of aromatic-amine dehydrogenase by 15N and 13C NMR.New insights into the multi-step reaction pathway of the reductive half-reaction catalysed by aromatic amine dehydrogenase: a QM/MM study.Importance of barrier shape in enzyme-catalyzed reactions. Vibrationally assisted hydrogen tunneling in tryptophan tryptophylquinone-dependent amine dehydrogenases.Active-site residues are critical for the folding and stability of methylamine dehydrogenase.Active site aspartate residues are critical for tryptophan tryptophylquinone biogenesis in methylamine dehydrogenase.Tryptophan tryptophylquinone cofactor biogenesis in the aromatic amine dehydrogenase of Alcaligenes faecalis. Cofactor assembly and catalytic properties of recombinant enzyme expressed in Paracoccus denitrificans.Incorporating Fast Protein Dynamics into Enzyme Design: A Proposed Mutant Aromatic Amine Dehydrogenase.Spectroscopic evidence for a common electron transfer pathway for two tryptophan tryptophylquinone enzymes.

P2860

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P2860

Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme.

http://www.wikidata.org/entity/Q36107587

description

1994 nî lūn-bûn

@nan

1994年の論文

@ja

1994年論文

@yue

1994年論文

@zh-hant

1994年論文

@zh-hk

1994年論文

@zh-mo

1994年論文

@zh-tw

1994年论文

@wuu

1994年论文

@zh

1994年论文

@zh-cn

name

Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme.

@ast

Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme.

@en

type

label

Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme.

@ast

Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme.

@en

prefLabel

Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme.

@ast

Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme.

@en

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P356

JB.176.10.2922-2929.1994

P1433

Journal of Bacteriology

P1476

Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme.

@en

P2093

A Y Chistoserdov

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

E Eisenstein

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

J Sanders-Loehr

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

L H Jones

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

S Govindaraj

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

S L Edwards

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

V L Davidson

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

P2860

Purification and properties of an amine dehydrogenase from Pseudomonas AM1 and its role in growth on methylamine

Microbial oxidation of amines. Spectral and kinetic properties of the primary amine dehydrogenase of Pseudomonas AM1

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Determination of the base composition of deoxyribonucleic acid from its thermal denaturation temperature

Cloning and sequencing of the structural gene for the small subunit of methylamine dehydrogenase from Methylobacterium extorquens AM1: evidence for two tryptophan residues involved in the active center.

The prosthetic group of methylamine dehydrogenase from Pseudomonas AM1: evidence for a quinone structure.

Crystallization and properties of aromatic amine dehydrogenase from Pseudomonas sp.

Purification and properties of methylamine dehydrogenase from Paracoccus denitrificans.

Distribution of membrane-bound monoamine oxidase in bacteria.

P304

2922-2929

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scholarly article

P356

10.1128/JB.176.10.2922-2929.1994

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10

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176

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1994-05-01T00:00:00Z

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8188594

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P932

205448

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