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The N-terminal domain of human holocarboxylase synthetase facilitates biotinylation via direct interaction with the substrate proteinBiotin synthesis in plants. The first committed step of the pathway is catalyzed by a cytosolic 7-keto-8-aminopelargonic acid synthaseCarboxylation mechanism and stereochemistry of crotonyl-CoA carboxylase/reductase, a carboxylating enoyl-thioester reductaseCrystal structure of biotin carboxylase in complex with substrates and implications for its catalytic mechanismLipoylating and biotinylating enzymes contain a homologous catalytic moduleA minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylationBiocatalysis for the application of CO2 as a chemical feedstockStructure and function of biotin-dependent carboxylasesTranscarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme coreCrystal structure of the carboxyltransferase subunit of the bacterial sodium ion pump glutaconyl-coenzyme A decarboxylaseN 5 -CAIR Mutase: Role of a CO 2 Binding Site and Substrate Movement in Catalysis † , ‡Protein biotinylation visualized by a complex structure of biotin protein ligase with a substrateMechanism for the inhibition of the carboxyltransferase domain of acetyl-coenzyme A carboxylase by pinoxadenStructural and Biochemical Studies on the Regulation of Biotin Carboxylase by Substrate Inhibition and DimerizationInteraction between the Biotin Carboxyl Carrier Domain and the Biotin Carboxylase Domain in Pyruvate Carboxylase from Rhizobium etliCharacterizing the Importance of the Biotin Carboxylase Domain Dimer for Staphylococcus aureus Pyruvate Carboxylase CatalysisAn unanticipated architecture of the 750-kDa α6β6 holoenzyme of 3-methylcrotonyl-CoA carboxylaseCrystal Structure of Urea Carboxylase Provides Insights into the Carboxyltransfer ReactionBiochemical and Structural Characterization of the Arabidopsis Bifunctional Enzyme Dethiobiotin Synthetase–Diaminopelargonic Acid Aminotransferase: Evidence for Substrate Channeling in Biotin SynthesisCrystal Structure of Carboxyltransferase from Staphylococcus aureus Bound to the Antibacterial Agent Moiramide BVhr1p, a new transcription factor from budding yeast, regulates biotin-dependent expression of VHT1 and BIO5.Biotin protein ligase from Saccharomyces cerevisiae. The N-terminal domain is required for complete activity.Identification of the plasma membrane H+-biotin symporter of Saccharomyces cerevisiae by rescue of a fatty acid-auxotrophic mutant.BiotinBiochemical characterization of the Arabidopsis biotin synthase reaction. The importance of mitochondria in biotin synthesisFrontiers, opportunities, and challenges in biochemical and chemical catalysis of CO2 fixationWheat acetyl-coenzyme A carboxylase: cDNA and protein structure.Functional conformations for pyruvate carboxylase during catalysis explored by cryoelectron microscopyStructure and function of a single-chain, multi-domain long-chain acyl-CoA carboxylase.Identification of the tRNA-binding protein Arc1p as a novel target of in vivo biotinylation in Saccharomyces cerevisiae.Acetyl-CoA carboxylase from Escherichia coli: gene organization and nucleotide sequence of the biotin carboxylase subunit.Probing the catalytic roles of Arg548 and Gln552 in the carboxyl transferase domain of the Rhizobium etli pyruvate carboxylase by site-directed mutagenesis.Analysis of gene evolution and metabolic pathways using the Candida Gene Order BrowserIscS functions as a primary sulfur-donating enzyme by interacting specifically with MoeB and MoaD in the biosynthesis of molybdopterin in Escherichia coliStructure, function and regulation of pyruvate carboxylase.The BioC O-methyltransferase catalyzes methyl esterification of malonyl-acyl carrier protein, an essential step in biotin synthesis.Remarkable diversity in the enzymes catalyzing the last step in synthesis of the pimelate moiety of biotin.Anaerobic transformation of alkanes to fatty acids by a sulfate-reducing bacterium, strain Hxd3Peroxisomes are involved in biotin biosynthesis in Aspergillus and Arabidopsis.Molecular cloning and characterization of the cDNA coding for the biotin-containing subunit of 3-methylcrotonoyl-CoA carboxylase: identification of the biotin carboxylase and biotin-carrier domains
P2860
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P2860
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
1989年论文
@zh
1989年论文
@zh-cn
name
The mechanism of biotin-dependent enzymes.
@en
type
label
The mechanism of biotin-dependent enzymes.
@en
prefLabel
The mechanism of biotin-dependent enzymes.
@en
P1476
The mechanism of biotin-dependent enzymes.
@en
P2093
Knowles JR
P304
P356
10.1146/ANNUREV.BI.58.070189.001211
P577
1989-01-01T00:00:00Z