PKM pyruvate kinase M1/2 [Oryctolagus cuniculus (rabbit)] - Gene

Summary

Gene symbol: PKM
Gene description: pyruvate kinase M1/2
See related: Ensembl:ENSOCUG00000006119
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Oryctolagus cuniculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus
Also known as: PKM2
Orthologs: human mouse all
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Genomic context

Location:: chromosome: 17

Exon count:: 14

Annotation release	Status	Assembly	Chr	Location
RS_2023_02	current	UM_NZW_1.0 (GCF_009806435.1)	17	NC_067390.1 (1302766..1326053)

Chromosome 17 - NC_067390.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_067390.1 Chromosome 17 Reference UM_NZW_1.0 Primary Assembly

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

A magneto-controlled biocatalytic cascade with a fluorescent output.
Title: A magneto-controlled biocatalytic cascade with a fluorescent output.
the polarity of the residue 113 is central in the partition of K+ into its site and that the substitution of Thr for Leu changes the ion selectivity for the monovalent cation with minor changes in the binding of the substrates.
Title: The importance of polarity in the evolution of the K+ binding site of pyruvate kinase.
In contrast to PK from rabbit tissues, the enzyme from the hare heart and muscles PK is presented by its allosteric isoform which might by advantageous under extreme conditions of the hare's habitation
Title: [Different properties of pyruvate kinase from rabbit and hare muscles].
Mass spectrometry has been used to determine the number of exchangeable backbone amide protons and the associated rate constants that are altered when PKM binds either the allosteric inhibitor phenylalanine or a nonallosteric analogue of the inhibitor.
Title: Identification of regions of rabbit muscle pyruvate kinase important for allosteric regulation by phenylalanine, detected by H/D exchange mass spectrometry.
Carboxyl group of the substrate phosphoenolpyruvate is responsible for energetic coupling with phenylalanine binding in the allosteric sites.
Title: Distinguishing the chemical moiety of phosphoenolpyruvate that contributes to allostery in muscle pyruvate kinase.
Bound mono- and divalent cations influence the binding of the substrate phosphoenolpyruvate to pyruvate kinase, in particular the binding-induced structural change of the protein and the conformation and interaction of bound phosphoenolpyruvate.
Title: Effects of ions on ligand binding to pyruvate kinase: mapping the binding site with infrared spectroscopy.
The structure of rabbit muscle pyruvate kinase-Mn-pyruvate-proline complex reported herein demonstrates that proline binds specifically to the allosteric site of muscle pyruvate kinase.
Title: The pyruvate kinase model system, a cautionary tale for the use of osmolyte perturbations to support conformational equilibria in allostery.
In the absence of substrate, SAXS-monitored conformational changes in muscle pyruvate kinase elicited by the binding of phenylalanine (an allosteric inhibitor) are similar to those observed upon binding of alanine or 2-aminobutyric acid.
Title: Changes in small-angle X-ray scattering parameters observed upon binding of ligand to rabbit muscle pyruvate kinase are not correlated with allosteric transitions.
Fluorescence study of muscle pyruvate kinase confirms an increase in the isobaric heat capacity associated with entropy-driven R --> T transition and an intriguing role of adenosine diphosphate (ADP) in the enzyme activation process.
Title: Functional energetic landscape in the allosteric regulation of muscle pyruvate kinase. 2. Fluorescence study.
Simulation of pyruvate kinase regulatory behavior under physiological conditions shows that the thermodynamics involved in the enzyme's regulation are well-tuned to allow maximal response to even minute changes in temperature and ligand concentration.
Title: Functional energetic landscape in the allosteric regulation of muscle pyruvate kinase. 3. Mechanism.

Submit: New GeneRIF Correction See all GeneRIFs (11)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Gene Ontology Provided by RefSeq

Function	Evidence Code	Pubs
enables magnesium ion binding	IEA Inferred from Electronic Annotation more info	PubMed
enables potassium ion binding	IEA Inferred from Electronic Annotation more info	PubMed
enables pyruvate kinase activity	IEA Inferred from Electronic Annotation more info	PubMed

Process	Evidence Code	Pubs
involved_in cellular response to insulin stimulus	IEA Inferred from Electronic Annotation more info	PubMed
involved_in glycolytic process	IEA Inferred from Electronic Annotation more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	IEA Inferred from Electronic Annotation more info	PubMed

General protein information

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Preferred Names: pyruvate kinase PKM

Names: ATP:pyruvate 2-o-phosphotransferase; Pyruvate kinase isozymes M1/M2; Pyruvate kinase muscle isozyme; pyruvate kinase, muscle; threonine-protein kinase PKM2; tyrosine-protein kinase PKM2

NP_001182573.1

EC 2.7.1.40

EC 2.7.10.2

EC 2.7.11.1

NP_001182574.1

EC 2.7.1.40

EC 2.7.10.2

EC 2.7.11.1

XP_051677658.1

EC 2.7.1.40

EC 2.7.10.2

EC 2.7.11.1

XP_051677659.1

EC 2.7.1.40

EC 2.7.10.2

EC 2.7.11.1

XP_051677660.1

EC 2.7.1.40

EC 2.7.10.2

EC 2.7.11.1

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001195644.1 → NP_001182573.1 pyruvate kinase PKM isoform 1

Status: VALIDATED

Description

Transcript Variant: This variant (1) uses an alternate in-frame exon in the 3' coding region compared to variant 2. The resulting protein (isoform 1) has a different internal segment but is the same length as isoform 2.

Source sequence(s)

U44751, VIYN02003006

UniProtKB/Swiss-Prot

O18919, P11974, Q29501

Related

ENSOCUP00000043306.1, ENSOCUT00000044057.1

Conserved Domains (2) summary

cd00288
Location:42 → 530

Pyruvate_Kinase; Pyruvate kinase (PK): Large allosteric enzyme that regulates glycolysis through binding of the substrate, phosphoenolpyruvate, and one or more allosteric effectors. Like other allosteric enzymes, PK has a high substrate affinity R state and a low ...

TIGR01064
Location:43 → 527

pyruv_kin; pyruvate kinase
NM_001195645.1 → NP_001182574.1 pyruvate kinase PKM isoform 2

Status: VALIDATED

Description

Transcript Variant: This variant (2) uses an alternate in-frame exon in the 3' coding region compared to variant 1. The resulting protein (isoform 2) has a different internal segment but is the same length as isoform 1.

Source sequence(s)

AF032389, VIYN02003006

UniProtKB/Swiss-Prot

O18919, P11974, Q29501

Related

ENSOCUP00000044499.1, ENSOCUT00000041853.1

Conserved Domains (2) summary

cd00288
Location:42 → 530

Pyruvate_Kinase; Pyruvate kinase (PK): Large allosteric enzyme that regulates glycolysis through binding of the substrate, phosphoenolpyruvate, and one or more allosteric effectors. Like other allosteric enzymes, PK has a high substrate affinity R state and a low ...

TIGR01064
Location:43 → 527

pyruv_kin; pyruvate kinase