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Title

Phosphoglycerate kinase acts as a futile cycle at high temperature

Authors

Theresa Kouril,1,2 Johann J. Eicher,2 Bettina Siebers1 and Jacky L. Snoep2,3,4,*

Affiliations

1Molecular Enzyme Technology and Biochemistry (MEB), BiofilmCentre, Faculty of Chemistry, University of Duisburg-Essen, Duisburg, Germany; 2Department of Biochemistry, Stellenbosch University, Private Bag X1, Matieland 7602, South Africa; 3Molecular Cell Physiology, Vrije Universiteit Amsterdam, Amsterdam, The Netherlands; 4MIB, University of Manchester, Manchester, UK.

Abstract

In (hyper)thermophilic organisms metabolic processes have to be adapted to function optimally at high temperature. We compared the gluconeogenetic conversion of 3-phosphoglycerate via 1,3-bisphosphoglycerate to glyceraldehyde-3-phosphate at 30 C and at 70 C. At 30 C it was possible to produce 1,3-bisphosphoglycerate from 3-phosphoglycerate, but at 70 C, 1,3- bisphosphoglycerate was dephosphorylated rapidly to 3-phosphoglycerate, effectively turning the phosphoglycerate kinase into a futile cycle. When phosphoglycerate kinase was incubated together with glyceraldehyde 3-phosphate dehydrogenase it was possible to convert 3-phosphoglycerate to glyceraldehyde 3-phosphate, both at 30 C and at 70 C, however, at 70 C only low concentrations of product were observed due to thermal instability of glyceraldehyde 3-phosphate. Thus, thermolabile intermediates challenge central metabolic reactions and require special adaptation strategies for life at high temperature.

Journal

Microbiology

Unit definitions have no effect on the numerical analysis of the model. It remains the responsibility of the modeler to ensure the internal numerical consistency of the model. If units are provided, however, the consistency of the model units will be checked.

Name Definition
Id Name Spatial dimensions Size
default 0.0 1.0
Id Name Initial quantity Compartment Fixed
ADP 0.0 default
ATP 10.0 default
BPG 0.0 default
GA 0.0 default
P3G 3.0 default
gap 0.0 default
glc 10.0 default
nadp 0.0 default
nadph 0.2 default
pep 5.0 default
pi 0.0 default
pyr 0.4 default
sink 0.0 default

Initial assignments are expressions that are evaluated at time=0. It is not recommended to create initial assignments for all model entities. Restrict the use of initial assignments to cases where a value is expressed in terms of values or sizes of other model entities. Note that it is not permitted to have both an initial assignment and an assignment rule for a single model entity.

Definition
Id Name Objective coefficient Reaction Equation and Kinetic Law Flux bounds
v1 ATP + P3G = ADP + BPG

protPGK * (-VmrPGK * ADP * BPG / (KpgkADP * KpgkBPG) + VmfPGK * ATP * P3G / (KpgkATP * KpgkP3G)) / ((1 + ADP / KiADP) * (1 + P3G / KpgkP3G * (1 + ATP / KpgkATP) + BPG / KpgkBPG * (1 + ADP / KpgkADP)))
v2 ADP + pep = ATP + pyr

kPK * ADP * pep
v3 BPG = pi + P3G

kdbpg * BPG
v4 nadph + BPG = pi + nadp + gap

protGAPdh * ((-Vmarev * (gap * nadp / (Kgap * Knadp)) * (pi / Kpi) + Vmfor * BPG * nadph / (KBPG * Knadph)) / ((1 + nadp / Knadp + nadph / Knadph) * ((1 + gap / Kgap) * (1 + pi / Kpi) + BPG / KBPG)))
v5 nadp + glc = nadph + GA

kGDH * glc * nadp
v6 gap = sink

kdgap * gap

Global parameters

Id Value
KBPG 0.0895997307185501
Kgap 3.09006
KiADP 1.01661161972841
Knadp 0.204381
Knadph 0.092444
KpgkADP 0.374683891073216
KpgkATP 9.30939957007288
KpgkBPG 0.00824346710166223
KpgkP3G 0.567800672197298
Kpi 112.39
Vmarev 35.871
VmfPGK 17.2125572084323
Vmfor 23.3991
VmrPGK 37.9602642543915
kGDH 10.0
kPK 50.0
kdbpg 0.736416
kdgap 0.0559
protGAPdh 0.0421
protPGK 0.0045
sink2 0.0

Local parameters

Id Value Reaction

Assignment rules

Definition

Rate rules

Definition

Algebraic rules

Definition
Trigger Assignments