Difference between revisions of "Pyk"

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|style="background:#ABCDEF;" align="center"|'''Function''' || catabolic enzyme in glycolysis
 
|style="background:#ABCDEF;" align="center"|'''Function''' || catabolic enzyme in glycolysis
 
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://cellpublisher.gobics.de/subtiexpress/ ''Subti''Express]''': [http://cellpublisher.gobics.de/subtiexpress/bsu/BSU29180 pyk]
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU29180 pyk]
 
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/carbon_flow.html Central C-metabolism]'''
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/carbon_flow.html Central C-metabolism]'''
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ytzA]]'', ''[[pfkA]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ytzA]]'', ''[[pfkA]]''
 
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|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB14878&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU29180 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU29180 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU29180 Advanced_DNA]
 
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|colspan="2" | '''Genetic context''' <br/> [[Image:pyk_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:pyk_context.gif]]

Revision as of 13:34, 13 May 2013

  • Description: pyruvate kinase, glycolytic enzyme

Gene name pyk
Synonyms pykA
Essential no
Product pyruvate kinase
Function catabolic enzyme in glycolysis
Gene expression levels in SubtiExpress: pyk
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism
MW, pI 61,9 kDa, 4.88
Gene length, protein length 1755 bp, 585 amino acids
Immediate neighbours ytzA, pfkA
Sequences Protein DNA Advanced_DNA
Genetic context
Pyk context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Pyk expression.png




























Categories containing this gene/protein

ATP synthesis, carbon core metabolism, phosphoproteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU29180

Phenotypes of a mutant

Unable to grow with non-PTS carbohydrates (such as glucitol or glycerol) as single carbon source.

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

  • A mutation was found in this gene after evolution under relaxed selection for sporulation PubMed

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ADP + phosphoenolpyruvate --> ATP + pyruvate
    • The reaction is irreversible under physiological conditions
  • Protein family: PEP-utilizing enzyme family (according to Swiss-Prot) pyruvate kinase family, (C-terminal section: PEP-utilizing enzyme family)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information: Allosteric Regulation PubMed
  • Domains:
  • Modification: phosphorylation on Ser36 PubMed, PubMed, phosphorylation on Ser536 or Ser546 PubMed, please note that the Ser is not on position 536 but rather at 538
  • Cofactor(s): Mg2+, K+
  • Effectors of protein activity:
    • Activated by PEP (Hill Coefficient 1,8) PubMed PubMed
    • Allosterically activated by AMP PubMed
    • Activation by r5p and ADP PubMed
    • Inhibition by ADP and f16bp in high concentrations; and ATP PubMed

Database entries

  • Structure: 2E28 (Geobacillus stearothermophilus)
  • KEGG entry: [3]

Additional information

The enzyme is a tetramer with four active sites PubMed

Expression and regulation

  • Sigma factor:
  • Regulation:
    • twofold induced by glucose PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • GP589 (pyk::cat), available in Stülke lab
  • GP600 (pyk::erm), available in Stülke lab
  • Expression vector:
    • expression in E. coli, N-terminal His-tag: pGP1100 (in pWH844), available in Stülke lab
    • expression in B. subtilis, native protein: pGP1411 (in pBQ200), available in Stülke lab
    • expression in B. subtilis, N-terminal Strep-tag: pGP1409 (in pGP380), available in Stülke lab
    • expression in B. subtilis, C-terminal Strep-tag: pGP1410 (in pGP382), available in Stülke lab
  • lacZ fusion: see pfkA
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
  • Antibody:

Labs working on this gene/protein

Jörg Stülke, University of Göttingen, Germany Homepage

Your additional remarks

References

Natividad Cabrera-Valladares, Luz M Martínez, Noemí Flores, Georgina Hernández-Chávez, Alfredo Martínez, Francisco Bolívar, Guillermo Gosset
Physiologic consequences of glucose transport and phosphoenolpyruvate node modifications in Bacillus subtilis 168.
J Mol Microbiol Biotechnol: 2012, 22(3);177-97
[PubMed:22846916] [WorldCat.org] [DOI] (I p)

Christopher T Brown, Laura K Fishwick, Binna M Chokshi, Marissa A Cuff, Jay M Jackson, Travis Oglesby, Alison T Rioux, Enrique Rodriguez, Gregory S Stupp, Austin H Trupp, James S Woollcombe-Clarke, Tracy N Wright, William J Zaragoza, Jennifer C Drew, Eric W Triplett, Wayne L Nicholson
Whole-genome sequencing and phenotypic analysis of Bacillus subtilis mutants following evolution under conditions of relaxed selection for sporulation.
Appl Environ Microbiol: 2011, 77(19);6867-77
[PubMed:21821766] [WorldCat.org] [DOI] (I p)

Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680] [WorldCat.org] [DOI] (P p)

Laurent Jannière, Danielle Canceill, Catherine Suski, Sophie Kanga, Bérengère Dalmais, Roxane Lestini, Anne-Françoise Monnier, Jérôme Chapuis, Alexander Bolotin, Marina Titok, Emmanuelle Le Chatelier, S Dusko Ehrlich
Genetic evidence for a link between glycolysis and DNA replication.
PLoS One: 2007, 2(5);e447
[PubMed:17505547] [WorldCat.org] [DOI] (I e)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)

Alain Lévine, Françoise Vannier, Cédric Absalon, Lauriane Kuhn, Peter Jackson, Elaine Scrivener, Valérie Labas, Joëlle Vinh, Patrick Courtney, Jérôme Garin, Simone J Séror
Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes.
Proteomics: 2006, 6(7);2157-73
[PubMed:16493705] [WorldCat.org] [DOI] (P p)

H Ludwig, G Homuth, M Schmalisch, F M Dyka, M Hecker, J Stülke
Transcription of glycolytic genes and operons in Bacillus subtilis: evidence for the presence of multiple levels of control of the gapA operon.
Mol Microbiol: 2001, 41(2);409-22
[PubMed:11489127] [WorldCat.org] [DOI] (P p)

B Fry, T Zhu, M M Domach, R R Koepsel, C Phalakornkule, M M Ataai
Characterization of growth and acid formation in a Bacillus subtilis pyruvate kinase mutant.
Appl Environ Microbiol: 2000, 66(9);4045-9
[PubMed:10966427] [WorldCat.org] [DOI] (P p)

H Sakai, K Suzuki, K Imahori
Purification and properties of pyruvate kinase from Bacillus stearothermophilus.
J Biochem: 1986, 99(4);1157-67
[PubMed:3711058] [WorldCat.org] [DOI] (P p)

M Diesterhaft, E Freese
Pyruvate kinase of bacillus subtilis.
Biochim Biophys Acta: 1972, 268(2);373-80
[PubMed:4623707] [WorldCat.org] [DOI] (P p)