About: Influence of Ligands on the Coenzyme Dissociation Constants in Octopine Dehydrogenase

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Influence of Ligands on the Coenzyme Dissociation Constants in Octopine Dehydrogenase Goto Sponge NotDistinct Permalink

An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

scientific article published on 01 July 1974

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в липні 1974 (uk) im Juli 1974 veröffentlichter wissenschaftlicher Artikel (de) scientific article published on 01 July 1974 (en) artículu científicu espublizáu en xunetu de 1974 (ast)
publication date	wds:Q57696204-02013225-25BE-4E57-A997-EC5FBF6A4E54
publication date	1974-07-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q57696204-AA10F163-9118-47C0-87A7-8AF5C14C4542
language of work or name	English
cites work	wds:Q57696204-10608BBD-5C7C-42C0-AB6B-B1F372505BF6 wds:Q57696204-BA1466FD-19C6-404C-BFBB-C0EB3CDD31C9 wds:Q57696204-FD4DC392-7953-4148-9ACF-94DE7C4B17DB
cites work	Equilibrium binding of nicotinamide nucleotides to lactate dehydrogenases Protein fluorescence of nicotinamide nucleotide-dependent dehydrogenases Octopine dehydrogenase. Purification and catalytic properties
author name string	wds:Q57696204-2C59637C-BDD5-461E-857E-4A94D6848C86 wds:Q57696204-45988D0D-3576-430D-B8E4-DCC70975ADCC wds:Q57696204-9A67F2BA-6FE3-4115-91F6-C352E0B30C27 wds:Q57696204-F9419FF0-A1B5-4A4C-8507-0BE35F549BE6
author name string	P L Luisi A Olomucki M O Doublet J Klincak
rdfs:label	Influence of Ligands on the Coenzyme Dissociation Constants in Octopine Dehydrogenase (en) Influence of Ligands on the Coenzyme Dissociation Constants in Octopine Dehydrogenase (nl)
skos:prefLabel	Influence of Ligands on the Coenzyme Dissociation Constants in Octopine Dehydrogenase (en) Influence of Ligands on the Coenzyme Dissociation Constants in Octopine Dehydrogenase (nl)
name	Influence of Ligands on the Coenzyme Dissociation Constants in Octopine Dehydrogenase (en) Influence of Ligands on the Coenzyme Dissociation Constants in Octopine Dehydrogenase (nl)
author	wds:Q57696204-7B3D1E2D-06CC-4E16-AD1D-4C2F8EF8531A
author	Antonio Baici
title	wds:Q57696204-B3F2F105-236D-42A9-AB74-25C3C95F7565
title	Influence of ligands on the coenzyme dissociation constants in octopine dehydrogenase (en)
page(s)	wds:Q57696204-4201A134-8B2D-43B6-B981-D351D4C76574
page(s)	59-66
instance of	wds:Q57696204-24E42D84-C800-40FB-A68C-05CAD956AE0C
instance of	scholarly article
PubMed ID	wds:Q57696204-8772E05C-36EF-44AB-95F4-45D46D7C5186
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/4368817
PubMed ID	4368817
published in	wds:Q57696204-FCBCFE93-760C-4A78-9254-04D4EE47A04A
published in	FEBS Journal
issue	wds:Q57696204-1931E136-5750-4486-B565-E82B37EAC6D5
volume	wds:Q57696204-AE486627-36F3-4292-9179-7ECF7F83568C
issue	1
volume	46
DOI	wds:Q57696204-CE858DE5-A00C-441B-AEDE-DFEA5210B841
DOI	http://dx.doi.org/10.1111/J.1432-1033.1974.TB03596.X
DOI	10.1111/J.1432-1033.1974.TB03596.X
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q57696204
is cites work of	Etheno-Substituted Nucleotides and Coenzymes: Fluorescence and Biological Activity Relation between fluorescence and conformation of iεNAD+bound to dehydrogenases Investigation on the Kinetic Mechanism of Octopine Dehydrogenase. A Regulatory Behavior Kinetic Characterization of Tissue-Specific Isozymes of Octopine Dehydrogenase from Mantle Muscle and Brain of Sepia officinalis. Functional Similarities to the M4 and H4 Isozymes of Lactate Dehydrogenase Insights into the mechanism of ligand binding to octopine dehydrogenase from Pecten maximus by NMR and crystallography Study of Coenzyme Binding Site of Octopine Dehydrogenase Using Analogues of NAD+ Circular Dichroic Properties and Conformation of Thionicotinamide Dinucleotides Bound to Horse-Liver Alcohol Dehydrogenase Investigations on the Kinetic Mechanism of Octopine Dehydrogenase. 1. Steady-State Kinetics Inactivation of yeast alcohol dehydrogenase by a reactive coenzyme analogue: 3-chloroacetyl pyridine adenine dinucleotide An ion-exchange column chromatographic method for the isolation of octopine from Sepia officinalis L. muscle Bromopyruvate, a potential affinity label for octopine dehydrogenase
is cites work of	wds:Q40210121-F5200642-C10C-4D21-8F90-34D9E4B80D7C wds:Q40134525-F0ADD1C0-C6B4-4B41-9F8C-A95EB001C5F1 wds:Q39067709-41563F72-527C-4FE6-BF49-87A53FB7F689 wds:Q40170260-A2D209F9-077A-4AB5-94DB-405204C87B92 wds:Q39923196-0D06BAEF-4504-49AA-A461-9A9505EC802D wds:Q40139797-91E3C0EA-A85A-40CF-8029-3FD67C486483 wds:Q39951943-C9060BC6-8874-4301-A263-27F0A01FB149 wds:Q21562170-69FA8D77-54EA-4F9C-B6B8-61117803528F wds:Q40825656-E0505B29-1DFB-4970-B478-C6F780F0721E wds:Q71638155-67F59F70-937B-48B1-B501-921C98C8C475 wds:Q93569248-527E1CB8-6241-4CAD-A20F-359179ACBF10

Faceted Search & Find service v1.16.117 as of May 05 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3239 as of May 5 2024, on Linux (x86_64-centos_6-linux-gnu), Single-Server Edition (378 GB total memory, 190 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software