GPMDB00635OtherWisniewski JRInstrumentNot AvailableNot availableMus_musculus_viruses, Mousejwisniew@biochem.mpg.de26080680http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210039809http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210039807http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210039808http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210039805http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210039806http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210039814http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210039803http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210039804http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210039801http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210039812http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210039813http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210039810http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210039799http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210039811http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210039800http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210039797http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210039798Biochemical Proteomics Group, Department of Proteomics and Signal Transduction, Max-Planck-Institute of BiochemistryNot availableGPMDBGlycolysis is the core metabolic pathway supplying energy to cells. Whereas the vast majority of studies focus on specific aspects of the process, global analyses characterizing simultaneously all enzymes involved in the process are scarce. Here, we demonstrate that quantitative label- and standard-free proteomics allows accurate determination of titers of metabolic enzymes and enables simultaneous measurements of titers and maximal enzymatic activities (Amax) of all glycolytic enzymes and the gluconeogenic fructose 1,6-bisphosphatase in mouse brain, liver and muscle. Despite occurrence of tissue-specific isoenzymes bearing different kinetic properties, the enzyme titers often correlated well with the Amax values. To provide a more general picture of energy metabolism, we analyzed titers of the enzymes in additional 7 mouse organs and in human cells. Across the analyzed samples, we identified two basic profiles: a "fast glucose uptake" one in brain and heart, and a "gluconeogenic rich" one occurring in liver. In skeletal muscles and other organs, we found intermediate profiles. Obtained data highlighted the glucose-flux-limiting role of hexokinase which activity was always 10- to 100-fold lower than the average activity of all other glycolytic enzymes. A parallel determination of enzyme titers and maximal enzymatic activities allowed determination of kcat values without enzyme purification. Results of our in-depth proteomic analysis of the mouse organs did not support the concepts of regulation of glycolysis by lysine acetylation.Integrating Proteomics and Enzyme Kinetics Reveals Tissue-Specific Types of the Glycolytic and Gluconeogenic Pathways.Wiśniewski Jacek R JR,Gizak Agnieszka A,Rakus Dariusz D,Wiśniewski Jacek R JR, Gizak Agnieszka A, Rakus Dariusz D, Rakus Dariusz Dtissue portion, Tissue, portion of tissue, simple tissue.3.4.22.-, data, Lysine Hydrochloride, Laboratory, AP-1, Mus domesticus, c-jun, acetylation, mouse, mini-ICE, CASP-14, House Mouse, results, mice C57BL/6xCBA/CaJ hybrid, Mus muscaris, Lysine Acetate, House, Mus, Acetate, Mini-ICE, proteomic analysis, Mus musculus domesticus, 2, Lysine, Mice, L-Lysine, L Lysine, Mus musculus, Junc, Caspase-14 subunit p10, Swiss, mice, Swiss Mouse, epsilon-diaminocaproic acid, House Mice, Swiss Mice, Caspase-14 subunit p19, alpha, C6H14N2O2, "mouse" EXACT common_name [], MICE, Laboratory Mice, domesticus, "house mouse" EXACT genbank_common_name [], "Mus muscaris" RELATED misnomer [], AP1, Lysin, c-Jun, "mice C57BL/6xCBA/CaJ hybrid" RELATED misspelling [], Mouse, house mouse, Acetylations., 6-diaminohexanoic acid, Proteomes, Laboratory Mouse, Enisyltissue portion, Tissue, portion of tissue, simple tissue.projections, Herz, Entire brain, muscle system, Lysine Hydrochloride, Laboratory, Isozymes, Ass-1, Metabolisms, Skeletal, Glukose, Mus domesticus, Embden-Meyerhof, Bioenergetics, adult heart, Monohydrate, CASP-14, (DL)-Isomer, Homo sapiense, Embden Meyerhof Parnas Pathway, House Mouse, temporal, circulatory vessel, Lysine Acetate, Levulosa Mein, Homo sapien, Roles, Homo sapians, AA408052, Dextrose, Concepts, fold, 2, Embden-Meyerhof Pathway, synganglion, Allozymes, Expenditure, L Lysine, average, portion of tissue, Muscle Tissues, Homo sapients, enzymes, heart or heart like organ, Tissue, iecur, epsilon-diaminocaproic acid, Pathways, Swiss Mice, suprasegmental levels of nervous system, cardiac structure, free, Fast, ASS, Muscles, Homo sapience, papilla, Lysin, Alloenzymes, Role Concepts, "mice C57BL/6xCBA/CaJ hybrid" RELATED misspelling [], house mouse, Home sapiens, FAST, vertebrate heart, dorsal tube, Levulose, Pathway, suprasegmental structures, anatomical protrusion, Levulosa, Levulosado Vitulia, set of muscles, acetylation, lamina, mouse, anaerobic glycolysis, flanges, set of skeletal muscles, FASTK, Normalcy, Embden-Meyerhof-Parnas, brain structure, results, mice C57BL/6xCBA/CaJ hybrid, Levulosado Braun, Embden-Meyerhof-Parnas Pathway, chambered heart, Role Concept, count, Homo sapian, Voluntary, Mini-ICE, shelf, Role, tissue portion, simple tissue, cardium, (alpha-D)-Isomer, Hexokinase A, L Glucose, Mus musculus, D-Glucose, Hexokinase D, Caspase-14 subunit p10, Levulosa Baxter, mice, shelves, Encephalon, motor system, Swiss Mouse, muscle organ - human, Caspase-14 subunit p19, alpha, ATP:D-hexose 6-phosphotransferase, MICE, projection, Homo sapines, ridge, Embden-Meyerhof pathway, human, muscle element, domesticus, MUSCLE VOLUNTARY, Energy Metabolisms, Health, L-Glucose, glycolysis, fructose, spine, D Glucose, Fructose, (L)-Isomer, Mouse, Acetylations., Glucose Monohydrate, Embden-Meyerhof Pathways, Levulosa Braun, Levulosado Bieffe Medit, the brain, Brain, gluco-hexose, 3.4.22.-, human being, Fleboplast, Entire heart, C6H12O6, Glucose, lamellae, Biocatalysts, Plast Apyr Levulosa Mein, adult somatic muscle, nucleocapsid, musculature system, number, STK10, muscles, branchial heart, mini-ICE, Encephalons, process of organ, presence, skeletal muscle, protrusion, jecur, lamella, Homo spaiens, House, Apir Levulosa, Metabolism, central nervous system, Fleboplast Levulosa, Mus musculus domesticus, MUSCLE SKELETAL, Lysine, Mice, Normalities, Nervous System, FOCUS, CNS, Brains, Swiss, Tissues, Levulosa Grifols, Energy, ridges, C6H14N2O2, Expenditures, "mouse" EXACT common_name [], Skeletal Muscles, man, muscule system, "Mus muscaris" RELATED misnomer [], cardiac pump, skeletal muscle cell, ATP:Fas-activated serine/threonine protein phosphotransferase activity, Homo sampiens, musculus, glucose uptake, laminae, Anterior Tibial, Anhydrous, modifed Embden-Meyerhof pathway, incidence, striated muscle, Hexokinase II, data, Embden Meyerhof Pathway, (beta-D)-Isomer, Skeletal muscle fiber, musculi, anatomical process, Entire liver, enzyme activity, Hearts, Muscle, encephalon, Cell, Mus muscaris, Concept, count in organism, somatic muscle, Apir, Mus, Acetate, heart, proteomic analysis, core, striated muscle cell, arabino-hex-2-ulose, Homo sapeins, L-Lysine, flange, organ process, Energy Expenditure, muscles set, Normality, Energy Expenditures, Humo sapiens, House Mice, muscle, Embden-Meyerhof-Parnas pathway, Bioenergetic, Anhydrous Dextrose, Levulosa Ife, Laboratory Mice, "house mouse" EXACT genbank_common_name [], process, processes, Livers, Homo spiens, Herz@de, "human" EXACT genbank_common_name [], Muscle organ, processus, musculature, quantitative, 6-diaminohexanoic acid, Levulosa Ibys, Muscle Tissue, Laboratory Mouse, Enisyl, muscle group, presence or absence in organism, skeletal muscle system, Glc6305http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210039797dbgap_ncbi~0patentfamilies~0rfam~0merops~0complex-portal~0uniprot~0wormbaseparasite~0embl-covid19~0reactome~0emdb~0wgs_masters~0ebiweb_resources~0opentargets_genetics~0biomodels_all~0ipd-mhc~0ebiweb_teams~0taxonomy~0genome_assembly~0sc-experiments~0ebiweb_people~0enzymeportal_enzymes~0ipd-nhkir~0cellosaurus~0pdbe~0chebi~0patentproteins~0interpro7~0uniref~0chembl~0pdbekb~0gpcrdb~0hgnc~0sc-genes~0intact~0rhea~0ebiweb_training~0alphafold~0imgt-hla~0patentnucleotides~0ensemblroot~0eva_studies~0non-coding~0europepmc~0pubmed~1identifiers_registry~0pdbechem~0hpa-covid19~0eva-variants-covid19~0biosamples~0gwas_catalog~0biotools~0tls_masters~0mesh~0coding~0sra~0opentargets~0efo~0embl-pathogen~0project~0pride~1human_diseases~0geo_datasets~0embl~0treefam~0uniparc~0ols~0dgva~0intenz~0go~0tsa_masters~0biosamples-covid19~0ebiweb_corporate~0omim~0lrg~0earlycause-molecular-sequences~0ipd-kir~0empiar~0rnacentral~0orcid_data_claims~0gpmdb~2lineage-covid19~0metagenomics~0pfam~0pride archive~1varsite~00Resource Reanalysis0.00.00.0194324491054904370.01.0falseIntegrating Proteomics and Enzyme Kinetics Reveals Tissue-Specific Types of the Glycolytic and Gluconeogenic Pathways.Data from ProteomeXchange, PXD ID: PXD002156. File: 20120523_EXQ4_JRW_SA_94_T_1.mzml. Published as part of J Proteome Res. 2015 Jun 16 . From the Abstract: {{i}} ...Results of our in-depth proteomic analysis of the mouse organs did not support the concepts of regulation of glycolysis by lysine acetylation. {{/i}}2015-06-22GPM1121003979726080680PXD002156PXD002156