Structure, mechanism and regulation of pyruvate carboxylase - Test2 - elhamkhani - TriplyDB

Structure, mechanism and regulation of pyruvate carboxylase

Structure, mechanism and regulation of pyruvate carboxylase

http://www.wikidata.org/entity/Q24632909

about

Nonstructural 5A protein of hepatitis C virus interacts with pyruvate carboxylase and modulates viral propagation Identification of FAH domain-containing protein 1 (FAHD1) as oxaloacetate decarboxylase A symmetrical tetramer for S. aureus pyruvate carboxylase in complex with coenzyme A The Role of TCA Cycle Anaplerosis in Ketosis and Fatty Liver in Periparturient Dairy Cows Regulation of the structure and activity of pyruvate carboxylase by acetyl CoA Structure and function of biotin-dependent carboxylases Chemistry and biochemistry of 13C hyperpolarized magnetic resonance using dynamic nuclear polarization FAH domain containing protein 1 (FAHD-1) is required for mitochondrial function and locomotion activity in C. elegans Structure and substrate selectivity of the 750-kDa α6β6 holoenzyme of geranyl-CoA carboxylase Interaction between the Biotin Carboxyl Carrier Domain and the Biotin Carboxylase Domain in Pyruvate Carboxylase from Rhizobium etli Characterizing the Importance of the Biotin Carboxylase Domain Dimer for Staphylococcus aureus Pyruvate Carboxylase Catalysis An unanticipated architecture of the 750-kDa α6β6 holoenzyme of 3-methylcrotonyl-CoA carboxylase Selective inhibition of Biotin Protein Ligase from Staphylococcus aureus Insights into the carboxyltransferase reaction of pyruvate carboxylase from the structures of bound product and intermediate analogs Mitochondrial protein acetylation as a cell-intrinsic, evolutionary driver of fat storage: chemical and metabolic logic of acetyl-lysine modifications Manganese homeostasis in the nervous system The ATP-grasp enzymes Manganese-induced Neurotoxicity: From C. elegans to Humans Pantothenate kinase 1 is required to support the metabolic transition from the fed to the fasted state Interaction of glutaric aciduria type 1-related glutaryl-CoA dehydrogenase with mitochondrial matrix proteins Oxamate Improves Glycemic Control and Insulin Sensitivity via Inhibition of Tissue Lactate Production in db/db Mice Frontiers, opportunities, and challenges in biochemical and chemical catalysis of CO2 fixation The co-chaperone DNAJC12 binds to Hsc70 and is upregulated by endoplasmic reticulum stress A genome-wide screen identifies PAPP-AA-mediated IGFR signaling as a novel regulator of habituation learning.The Concise Guide to PHARMACOLOGY 2013/14: enzymes.Functional conformations for pyruvate carboxylase during catalysis explored by cryoelectron microscopy Structure and function of a single-chain, multi-domain long-chain acyl-CoA carboxylase.Early evolution of the biotin-dependent carboxylase family.Toward understanding the impacts of sediment contamination on a native fish species: transcriptional effects, EROD activity, and biliary PAH metabolites Probing the catalytic roles of Arg548 and Gln552 in the carboxyl transferase domain of the Rhizobium etli pyruvate carboxylase by site-directed mutagenesis.Biotin analogues with antibacterial activity are potent inhibitors of biotin protein ligase.Δ9-THC increases endogenous AHA1 expression in rat cerebellum and may modulate CB1 receptor function during chronic use Regulation of pyruvate metabolism and human disease Stable isotope-resolved metabolomic analysis of lithium effects on glial-neuronal metabolism and interactions My favorite pyruvate carboxylase.Quaternary structure of the oxaloacetate decarboxylase membrane complex and mechanistic relationships to pyruvate carboxylases.The cyclic dinucleotide c-di-AMP is an allosteric regulator of metabolic enzyme function Cryo-EM analysis reveals new insights into the mechanism of action of pyruvate carboxylase.The role of biotin and oxamate in the carboxyltransferase reaction of pyruvate carboxylase Mechanisms of inhibition of Rhizobium etli pyruvate carboxylase by L-aspartate

P2860

Q24309143-DBA9DEFD-7B41-4C15-87EB-C9472FD2638D Q24313315-F0A86AF9-9758-4D5E-934A-7E3EACAC872A Q24647517-58F496EA-027A-4726-9F64-E8DAE8C28A97 Q26781843-FB6B18E8-0A8A-41C0-8E93-F6E306307F3F Q26829137-B213D404-76C7-4553-A4B3-2A9C80967389 Q26851762-4BBA68FC-5CEF-47D5-B50A-04385A747E81 Q27023363-23116B53-F69F-457A-8D21-C5D1099C87B1 Q27301461-BC38FE88-2F12-4F52-99C3-EBC32A5CA7C2 Q27316802-2311D4FD-48D7-4DB7-B037-8F47B2B5FD88 Q27674591-71C63EE6-A39E-4569-A804-24E5A3978992 Q27675725-D30F655D-15C0-4E80-9AB2-84084A62189A Q27676114-AB489955-8719-47C4-97FE-8B51B9841E29 Q27678137-7FF3FBF6-EF45-4002-AF7E-08536E97A717 Q27680459-02D0BD3E-BA7A-4C9F-B5FD-FAF5C8BD5DB6 Q27694582-23879F3A-553F-4369-8085-36D007FFDBB0 Q28080482-39AFD21C-19E2-4801-82C0-0522892EE37E Q28248129-6D63E191-A846-478F-A7DF-FF1097CB6543 Q28391985-0EEDD519-CDAF-4CCB-920E-1D265E903852 Q28474360-ECB6C14A-1897-495A-8097-4778E5AC2E9D Q28539440-AD46314A-AC8D-4658-BFF2-D13A83EA66E9 Q28550524-9673A78E-CE22-49CA-8D89-7CC62E511E22 Q28660533-92CBBED9-70F9-4EDA-9757-AFD887785548 Q30090221-68AC69EA-C476-4722-B765-0153EC0A6D86 Q30388151-C81BC80B-7AA6-47F0-9F1D-12CB17EC50BD Q30486745-F1AE1B72-E0C0-4673-97D6-F3DE11E16E22 Q30583334-E24C1D62-3DC3-456B-805A-AF2E61FD25B6 Q30619830-6B11B943-ED4A-46DF-ACDB-7243FF7A663C Q31029345-A64BF199-4ACB-475D-9B09-A7184F179CB7 Q31150556-430A59C7-BBCB-482C-9E68-A768ED01CD5B Q33540779-15C17E6C-246C-493A-9DE2-06F40D3219B6 Q33630509-DF8956CE-1EAB-4656-B6C1-DEC82F3F298B Q33723564-29386923-5E3C-4F2F-A0B7-E2C57856F4A8 Q33764544-716C32A8-3F86-460F-993F-78AE5B0383D0 Q33989596-4DD61B77-ECBB-47F9-BF01-0CA6070CB567 Q34157270-BBF19579-98F5-4559-AA1F-9E7804CB1709 Q34157671-E541EAFF-69ED-41F9-8A9C-11FF4DE0DA04 Q34199004-6C37D809-EE7B-4A63-96B2-3E9889160098 Q34205689-1D09D134-E5B5-4B1F-9777-C70F0D3F2716 Q34339082-51807274-3953-44E0-AAF0-0E6E915D707F Q34548596-DAD57CEB-26C8-459B-9CF9-330756B9C4DC

P2860

Structure, mechanism and regulation of pyruvate carboxylase

http://www.wikidata.org/entity/Q24632909

description

2008 nî lūn-bûn

@nan

2008 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2008年の論文

@ja

2008年論文

@yue

2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

name

Structure, mechanism and regulation of pyruvate carboxylase

@ast

Structure, mechanism and regulation of pyruvate carboxylase

@en

Structure, mechanism and regulation of pyruvate carboxylase

@nl

type

label

Structure, mechanism and regulation of pyruvate carboxylase

@ast

Structure, mechanism and regulation of pyruvate carboxylase

@en

Structure, mechanism and regulation of pyruvate carboxylase

@nl

prefLabel

Structure, mechanism and regulation of pyruvate carboxylase

@ast

Structure, mechanism and regulation of pyruvate carboxylase

@en

Structure, mechanism and regulation of pyruvate carboxylase

@nl

P1433

Q24632909-9B6B32D4-1A44-4112-98CD-0D92E69120D0

P1476

Q24632909-13CFA1D6-DC3A-462A-B0D7-68A9D4800346

P2093

Q24632909-2EAD0380-27CF-4465-A6BC-192F65DBDCFB

Q24632909-8565DA37-4403-4F61-A61C-270B53509B08

Q24632909-B17332AD-3922-418D-A1C7-D6A93AFBAD37

Q24632909-C4D16A84-198B-44DA-BE33-AEF20341D15E

Q24632909-E9F24F72-AC64-4667-B22D-636B7E806F50

P2860

Q24632909-013CF2AD-09EE-46C3-BD0D-7CCAF3769FD1

Q24632909-01641A75-92C1-4163-A1BB-4A91E7CBF62D

Q24632909-0269680B-4AAF-48B1-92DE-ED5FAC96A817

Q24632909-06F6908F-6349-4373-BED8-C24CA2CFE200

Q24632909-0702148F-A573-47D3-9EEF-665603CB3B38

Q24632909-080D37FF-E87F-47B9-8220-9C97D5AAC31C

Q24632909-086ACBD7-B3A1-4997-AFBE-F1E41C41F0AC

Q24632909-09EC1A73-812C-45E1-8A0F-0DE6504BBA72

Q24632909-11F36541-1E6A-4220-A308-EB21F5F15F18

Q24632909-15B09D77-902C-43C6-BEC6-5D33C03C2FBA

P304

Q24632909-5D5AB848-F837-4876-B413-5B693514024F

P31

Q24632909-6217F3F5-6381-4589-B608-D9D664C89EEE

P3181

Q24632909-B96268B7-08E5-47ED-8C8D-A193F35D582B

P356

Q24632909-B449DA55-9F4B-4FAE-9678-E60A602F1875

P407

Q24632909-045E8577-FDDE-4D88-A10D-CB84C8621059

P433

Q24632909-5DCAC7C3-2014-483F-A167-57C67F0B6261

P478

Q24632909-A454248D-4924-406E-ADC9-EDB421E72B6B

P50

Q24632909-51116ED9-0964-4BB6-9F1F-913EB8F226B9

P577

Q24632909-DC05562B-8F4C-4739-BDCA-AFF65E1D41DC

P698

Q24632909-A182FAA9-C53A-40DB-AB90-2F210EB06E7B

P921

Q24632909-0D1F3789-108F-42E9-91BA-218D98104721

Q24632909-433F630F-54AC-4E48-BA95-5D7773CC2FAF

P932

Q24632909-2F159134-9480-4675-BD5B-5BF30F7F1E22

P3181

P356

P1433

Biochemical Journal

P1476

Structure, mechanism and regulation of pyruvate carboxylase

@en

P2093

John C Wallace

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

Martin St Maurice

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

Paul V Attwood

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

Sarawut Jitrapakdee

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

W Wallace Cleland

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

P2860

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

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

Solution structures of apo and holo biotinyl domains from acetyl coenzyme A carboxylase of Escherichia coli determined by triple-resonance nuclear magnetic resonance spectroscopy

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

Crystal structure of the carboxyltransferase domain of the oxaloacetate decarboxylase Na+ pump from Vibrio cholerae

Structure of the biotin carboxylase domain of pyruvate carboxylase from Bacillus thermodenitrificans

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

Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase

Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing

P304

369-87

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

P31

scholarly article

P3181

3121189

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

P356

10.1042/BJ20080709

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

P407

P433

3

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

P478

413

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

P50

P577

2008-08-01T00:00:00Z

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

P698

18613815

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

P921

acetyl coenzyme a

P932

2859305

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