Conformational drift of dissociated lactate dehydrogenases

King, Lan; Weber, Gregorio

doi:10.1021/bi00360a023

Cited by 108 publications

(80 citation statements)

References 9 publications

(10 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In similar experiments, Weber and coworkers reported hysteresis phenomena ('conformational drift') and non-classical behaviour termed 'deterministic equilibrium' (King and Weber, 1986;Ruan and Weber, 1989;Erijman and Weber, 1991). This is to describe the finding that 'equilibrium' dissociation constants depend on concentration and differ (Seifert et al 1985).…”

Section: Pressure-dependent Dissociation-associationmentioning

confidence: 95%

Proteins under pressure

Groß

Jaenicke

1994

European Journal of Biochemistry

659

393

View full text Add to dashboard Cite

Oceans not only cover the major part of the earth's surface but also reach into depths exceeding the height of the Mt Everest. They are populated down to the deepest levels (=11800 m), which means that a significant proportion of the global biosphere is exposed to pressures of up to 120 MPa. Although this fact has been known for more than a century, the ecology of the 'abyss' is still in its infancy. Only recently, barophilic adaptation, i.e. the requirement of elevated pressure for viability, has been firmly established. In non-adapted organisms, increased pressure leads to morphological anomalies or growth inhibition, and ultimately to cell death. The detailed molecular mechanism of the underlying 'metabolic dislocation' is unresolved.Effects of pressure as a variable in microbiology, biochemistry and biotechnology allow the structure/function relationship of proteins and protein conjugates to be analyzed. In this context, stabilization by cofactors or accessory proteins has been observed. High-pressure equipment available today allows the comprehensive characterization of the behaviour of proteins under pressure. Single-chain proteins undergo pressure-induced denaturation in the 100-MPa range, which, in the case of oligomeric proteins or protein assemblies, is preceded by dissociation at lower pressure. The effects may be ascribed to the positive reaction volumes connected with the formation of hydrophobic and ionic interactions. In addition, the possibility of conformational effects exerted by moderate, non-denaturing pressures, and related to the intrinsic compressibility of proteins, is discussed. Crystallization may serve as a model reaction of protein self-organization. Kinetic aspects of its pressureinduced inhibition can be described by a model based on the Oosawa theory of molecular association. Barosensitivity is known to be correlated with the pressure-induced inhibition of protein biosynthesis. Attempts to track down the ultimate cause in the dissociation of ribosomes have revealed remarkable stabilization of functional complexes under pseudo-physiological conditions, with the post-translational complex as the most pressure-sensitive species. Apart from the key issue of barosensitivity and barophilic adaptation, high-pressure biochemistry may provide means to develop new approaches to nonthermic industrial processes, especially in the field of food technology.Life in the deep sea faces a whole set of unfavourable conditions, including pressures up to 120 MPa (1200 bar), temperatures around 2°C or, in volcanic regions, above 1OO"C, absence of sunlight, and scarce supply of organic nutrients. When 'deep' means deeper than 1000 m, these biotopes include more than half (~6 2 % ) of the volume of the global biosphere (Jannasch and Taylor, 1984). The average pressure on the ocean floor is of the order of 38 MPa, indicatCorrespondence to R. Jaenicke,

show abstract

Section: Pressure-dependent Dissociation-associationmentioning

confidence: 95%

Proteins under pressure

Groß

Jaenicke

1994

European Journal of Biochemistry

659

393

View full text Add to dashboard Cite

show abstract

“…In most cases the loss of activity is followed by dissociation into monomers, a process which can be reversed by rewarming; but in some cases it is followed by an aggregation step. 9,10,14 Reversible cold inactivation is believed to be of physiological significance. For example, tetramer-dimer equilibrium of phosphofructokinase was suggested as a factor responsible for a relative decrease in the contribution of glycolysis to overall energy production during hibernation in ground squirrels and European hamsters.…”

Section: Cold Inactivationmentioning

confidence: 99%

Structural insights into cold inactivation of tryptophanase and cold adaptation of subtilisin S41

et al. 2007

View full text Add to dashboard Cite

A wide variety of enzymes can undergo a reversible loss of activity at low temperature, a process that is termed cold inactivation. This phenomenon is found in oligomeric enzymes such as tryptophanase (Trpase) and other pyridoxal phosphate dependent enzymes. On the other hand, cold‐adapted, or psychrophilic enzymes, isolated from organisms able to thrive in permanently cold environments, have optimal activity at low temperature, which is associated with low thermal stability. Since cold inactivation may be considered “contradictory” to cold adaptation, we have looked into the amino acid sequences and the crystal structures of two families of enzymes, subtilisin and tryptophanase. Two cold adapted subtilisins, S41 and subtilisin‐like protease from Vibrio, were compared to a mesophilic and a thermophilic subtilisins, as well as to four PLP‐dependent enzymes in order to understand the specific surface residues, specific interactions, or any other molecular features that may be responsible for the differences in their tolerance to cold temperatures. The comparison between the psychrophilic and the mesophilic subtilisins revealed that the cold adapted subtilisins have a high content of acidic residues mainly found on their surface, making it charged. The analysis of the Trpases showed that they have a high content of hydrophobic residues on their surface. Thus, we suggest that the negatively charged residues on the surface of the subtilisins may be responsible for their cold adaptation, whereas the hydrophobic residues on the surface of monomeric Trpase molecules are responsible for the tetrameric assembly, and may account for their cold inactivation and dissociation. © 2007 Wiley Periodicals, Inc. Biopolymers 89: 354–359, 2008.This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

show abstract

“…Tetrameric forms of the enzymes from various tissues consist either of four identical subunits (M 4 or H 4 ) or of M and H subunits in different proportions (M 3 H, M 2 H 2 , MH 3 ) [4,5]. Enzymatic activity has been confirmed for the tetrameric and dimeric forms of LDH [7], while the activity of the monomer of the enzyme is contradictory [7,8]. Each subunit (monomer) of the enzyme consists of about 330 amino acids.…”

Section: Introductionmentioning

confidence: 99%

Ultracentrifugation studies of the location of the site involved in the interaction of pig heart lactate dehydrogenase with acidic phospholipids at low pH. A comparison with the muscle form of the enzyme

Terlecki

Czapińska

Hotowy

2007

Cellular and Molecular Biology Letters

View full text Add to dashboard Cite

Lactate dehydrogenase (LDH) from the pig heart interacts with liposomes made of acidic phospholipids most effectively at low pH, close to the isoelectric point of the protein (pH = 5.5). This binding is not observed at neutral pH or high ionic strength. LDH-liposome complex formation requires an absence of nicotinamide adenine dinucleotides and adenine nucleotides in the interaction environment. Their presence limits the interaction of LDH with liposomes in a concentration-dependent manner. This phenomenon is not observed for pig skeletal muscle LDH. The heart LDH-liposome complexes formed in the absence of nicotinamide adenine dinucleotides and adenine nucleotides are stable after the addition of these substances even in millimolar concentrations. The LDH substrates and studied nucleotides that inhibit the interaction of pig heart LDH with acidic liposomes can be ordered according to their effectiveness as follows: NADH > NAD > ATP = ADP > AMP > pyruvate. The phosphorylated form of NAD (NADP), nonadenine nucleotides (GTP, CTP, UTP) and lactate are ineffective. Chemically cross-linked pig heart LDH, with a tetrameric structure stable at low pH, behaves analogously to the unmodified enzyme, which excludes the participation of the interfacing parts of subunits in the interaction with acidic phospholipids. The presented results indicate that in lowered pH conditions, the NADH-cofactor binding site of pig heart LDH is strongly involved in the interaction of the enzyme with acidic phospholipids.

show abstract

Conformational drift of dissociated lactate dehydrogenases

Cited by 108 publications

References 9 publications

Proteins under pressure

Proteins under pressure

Structural insights into cold inactivation of tryptophanase and cold adaptation of subtilisin S41

Ultracentrifugation studies of the location of the site involved in the interaction of pig heart lactate dehydrogenase with acidic phospholipids at low pH. A comparison with the muscle form of the enzyme

Contact Info

Product

Resources

About