Interaction between the Biotin Carboxyl Carrier Domain and the Biotin Carboxylase Domain in Pyruvate Carboxylase from Rhizobium etli - Wikidata - awgldk - TriplyDB

Interaction between the Biotin Carboxyl Carrier Domain and the Biotin Carboxylase Domain in Pyruvate Carboxylase from Rhizobium etli

Interaction between the Biotin Carboxyl Carrier Domain and the Biotin Carboxylase Domain in Pyruvate Carboxylase from Rhizobium etli

http://www.wikidata.org/entity/Q27674591

about

Structure and function of biotin-dependent carboxylases The Structure of Allophanate Hydrolase from Granulibacter bethesdensis Provides Insights into Substrate Specificity in the Amidase Signature Family Characterizing the Importance of the Biotin Carboxylase Domain Dimer for Staphylococcus aureus Pyruvate Carboxylase Catalysis The Three-Dimensional Structure of the Biotin Carboxylase-Biotin Carboxyl Carrier Protein Complex of E. coli Acetyl-CoA Carboxylase A Substrate-induced Biotin Binding Pocket in the Carboxyltransferase Domain of Pyruvate Carboxylase Insights into the carboxyltransferase reaction of pyruvate carboxylase from the structures of bound product and intermediate analogs Functional conformations for pyruvate carboxylase during catalysis explored by cryoelectron microscopy The role of biotin and oxamate in the carboxyltransferase reaction of pyruvate carboxylase Mechanisms of inhibition of Rhizobium etli pyruvate carboxylase by L-aspartate Activation and inhibition of pyruvate carboxylase from Rhizobium etli.Novel insights into the biotin carboxylase domain reactions of pyruvate carboxylase from Rhizobium etli.Structural Analysis of Substrate, Reaction Intermediate, and Product Binding in Haemophilus influenzae Biotin Carboxylase Roles of Arg427 and Arg472 in the binding and allosteric effects of acetyl CoA in pyruvate carboxylase Allosteric regulation of the biotin-dependent enzyme pyruvate carboxylase by acetyl-CoA.The enzymes of biotin dependent CO₂ metabolism: what structures reveal about their reaction mechanisms.Nearly 50 years in the making: defining the catalytic mechanism of the multifunctional enzyme, pyruvate carboxylase.Coordinating role of His216 in MgATP binding and cleavage in pyruvate carboxylase.The urea carboxylase and allophanate hydrolase activities of urea amidolyase are functionally independent.Insights into molecular assembly of ACCase heteromeric complex in Chlorella variabilis--a homology modelling, docking and molecular dynamic simulation study.Allosteric regulation alters carrier domain translocation in pyruvate carboxylase.

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P2860

Interaction between the Biotin Carboxyl Carrier Domain and the Biotin Carboxylase Domain in Pyruvate Carboxylase from Rhizobium etli

http://www.wikidata.org/entity/Q27674591

description

2011 nî lūn-bûn

@nan

2011 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Interaction between the Biotin ...... arboxylase from Rhizobium etli

@ast

Interaction between the Biotin ...... arboxylase from Rhizobium etli

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Interaction between the Biotin ...... arboxylase from Rhizobium etli

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type

label

Interaction between the Biotin ...... arboxylase from Rhizobium etli

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Interaction between the Biotin ...... arboxylase from Rhizobium etli

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Interaction between the Biotin ...... arboxylase from Rhizobium etli

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Interaction between the Biotin ...... arboxylase from Rhizobium etli

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Interaction between the Biotin ...... arboxylase from Rhizobium etli

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Interaction between the Biotin ...... arboxylase from Rhizobium etli

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Interaction between the Biotin ...... arboxylase from Rhizobium etli

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Adam D Lietzan

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

Ann L Menefee

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John C Wallace

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Martin St Maurice

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Paul V Attwood

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Sudhanshu Kumar

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Tonya N Zeczycki

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W Wallace Cleland

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P2860

13C NMR isotopomer analysis reveals a connection between pyruvate cycling and glucose-stimulated insulin secretion (GSIS)

Structure, mechanism and regulation of pyruvate carboxylase

A symmetrical tetramer for S. aureus pyruvate carboxylase in complex with coenzyme A

Crystal structure of biotin carboxylase in complex with substrates and implications for its catalytic mechanism

A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity

Movement of the biotin carboxylase B-domain as a result of ATP binding

Domain architecture of pyruvate carboxylase, a biotin-dependent multifunctional enzyme

Crystal structures of human and Staphylococcus aureus pyruvate carboxylase and molecular insights into the carboxyltransfer reaction

Structural evidence for substrate-induced synergism and half-sites reactivity in biotin carboxylase

Crystal structure of the α6β6 holoenzyme of propionyl-coenzyme A carboxylase

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9708-23

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scholarly article

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10.1021/BI201277J

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45

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50

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