Difference between revisions of "Pyk"

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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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|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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|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 DNA_with_flanks]
 
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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 10:59, 14 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 DNA_with_flanks
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