PMID- 27815924
OWN - NLM
STAT- MEDLINE
DCOM- 20170907
LR  - 20221207
IS  - 0065-2598 (Print)
IS  - 0065-2598 (Linking)
VI  - 925
DP  - 2017
TI  - The Simple and Unique Allosteric Machinery of Thermus caldophilus Lactate 
      Dehydrogenase : Structure-Function Relationship in Bacterial Allosteric LDHs.
PG  - 117-145
LID - 10.1007/5584_2016_171 [doi]
AB  - Many bacterial L-lactate dehydrogenases (LDH) are allosteric enzymes, and usually 
      activated by fructose 1,6-bisphosphate (FBP) and often also by substrate 
      pyruvate. The active and inactive state structures demonstrate that Thermus 
      caldophilus, Lactobacillus casei, and Bifidobacterium longum LDHs consistently 
      undergo allosteric transition according to Monod-Wyman-Changeux model, where the 
      active (R) and inactive (T) states of the enzymes coexist in an allosteric 
      equilibrium (pre-existing equilibrium) independently of allosteric effectors. The 
      three enzymes consistently take on open and closed conformations of the 
      homotetramers for the T and R states, coupling the quaternary structural changes 
      with the structural changes in binding sites for substrate and FBP though 
      tertiary structural changes. Nevertheless, the three enzymes undergo markedly 
      different structural changes from one another, indicating that there is a high 
      variety in the allosteric machineries of bacterial LDHs. L. casei LDH undergoes 
      the largest quaternary structural change in the three enzymes, and regulates its 
      catalytic activity though a large linkage frame for allosteric motion. In 
      contrast, T. caldophilus LDH exhibits the simplest allosteric motion in the three 
      enzymes, involving a simple mobile structural core for the allosteric motion. 
      TcLDH likely mediates its allosteric equilibrium mostly through electrostatic 
      repulsion within the protein molecule, providing an insight for regulation 
      machineries in bacterial allosteric LDHs.
FAU - Taguchi, Hayao
AU  - Taguchi H
AD  - Department of Applied Biological Science, Faculty of Science and Technology, 
      Tokyo University of Science, 2641 Yamazaki, Noda, Chiba, 278-8510, Japan. 
      htaguchi@rs.noda.tus.ac.jp.
LA  - eng
PT  - Journal Article
PT  - Review
PL  - United States
TA  - Adv Exp Med Biol
JT  - Advances in experimental medicine and biology
JID - 0121103
RN  - 0 (Bacterial Proteins)
RN  - 0 (Fructosediphosphates)
RN  - 0 (Protein Subunits)
RN  - 8558G7RUTR (Pyruvic Acid)
RN  - EC 1.1.1.27 (L-Lactate Dehydrogenase)
RN  - M7522JYX1H (fructose-1,6-diphosphate)
SB  - IM
MH  - Allosteric Regulation
MH  - Bacterial Proteins/*chemistry/genetics/metabolism
MH  - Bifidobacterium longum/chemistry/*enzymology/genetics
MH  - Binding Sites
MH  - Fructosediphosphates/*chemistry/metabolism
MH  - Gene Expression
MH  - Kinetics
MH  - L-Lactate Dehydrogenase/*chemistry/genetics/metabolism
MH  - Lacticaseibacillus casei/chemistry/*enzymology/genetics
MH  - Models, Molecular
MH  - Protein Binding
MH  - Protein Interaction Domains and Motifs
MH  - Protein Structure, Quaternary
MH  - Protein Subunits/chemistry/genetics/metabolism
MH  - Pyruvic Acid/*chemistry/metabolism
MH  - Species Specificity
MH  - Structure-Activity Relationship
MH  - Substrate Specificity
MH  - Thermus/chemistry/*enzymology/genetics
OTO - NOTNLM
OT  - Allostery
OT  - L-Lactate dehydrogenase
OT  - Lactic bacteria
OT  - Monod-Wyman-Changeux model
OT  - Pre-existence equilibrium
OT  - Thermophilic bacteria
EDAT- 2016/11/07 06:00
MHDA- 2017/09/08 06:00
CRDT- 2016/11/06 06:00
PHST- 2016/11/07 06:00 [pubmed]
PHST- 2017/09/08 06:00 [medline]
PHST- 2016/11/06 06:00 [entrez]
AID - 10.1007/5584_2016_171 [doi]
PST - ppublish
SO  - Adv Exp Med Biol. 2017;925:117-145. doi: 10.1007/5584_2016_171.