5NQQ

Rabbit Muscle L-lactate dehydrogenase in complex with NADH and oxaloacetate

5NQQ の概要

• エントリーDOI: 10.2210/pdb5nqq/pdb
• 関連するPDBエントリー: 5NQB
• 分子名称: L-lactate dehydrogenase A chain, 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: oxaloacetate, oxidoreductase
• 由来する生物種: Oryctolagus cuniculus (Rabbit)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 149702.33

構造登録者

Luisi, B.F.,Olin-Sandoval, V. (登録日: 2017-04-20, 公開日: 2017-06-07, 最終更新日: 2024-01-17)

主引用文献

Alam, M.T.,Olin-Sandoval, V.,Stincone, A.,Keller, M.A.,Zelezniak, A.,Luisi, B.F.,Ralser, M.
The self-inhibitory nature of metabolic networks and its alleviation through compartmentalization.
Nat Commun, 8:16018-16018, 2017

PubMed Abstract: Metabolites can inhibit the enzymes that generate them. To explore the general nature of metabolic self-inhibition, we surveyed enzymological data accrued from a century of experimentation and generated a genome-scale enzyme-inhibition network. Enzyme inhibition is often driven by essential metabolites, affects the majority of biochemical processes, and is executed by a structured network whose topological organization is reflecting chemical similarities that exist between metabolites. Most inhibitory interactions are competitive, emerge in the close neighbourhood of the inhibited enzymes, and result from structural similarities between substrate and inhibitors. Structural constraints also explain one-third of allosteric inhibitors, a finding rationalized by crystallographic analysis of allosterically inhibited L-lactate dehydrogenase. Our findings suggest that the primary cause of metabolic enzyme inhibition is not the evolution of regulatory metabolite-enzyme interactions, but a finite structural diversity prevalent within the metabolome. In eukaryotes, compartmentalization minimizes inevitable enzyme inhibition and alleviates constraints that self-inhibition places on metabolism.

PubMed: 28691704
DOI: 10.1038/ncomms16018

実験手法

X-RAY DIFFRACTION (1.872 Å)