Difference between revisions of "Pyk"
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=== Basic information/ Evolution === | === Basic information/ Evolution === | ||
| − | * '''Catalyzed reaction/ biological activity:''' ATP + pyruvate | + | * '''Catalyzed reaction/ biological activity:'''ADP + phosphoenolpyruvate --> ATP + pyruvate, the reaction is irreversible under physiological conditions |
* '''Protein family:''' pyruvate kinase family, (C-terminal section: PEP-utilizing enzyme family) | * '''Protein family:''' pyruvate kinase family, (C-terminal section: PEP-utilizing enzyme family) | ||
Revision as of 17:57, 14 January 2009
- Description: pyruvate kinase, glycolytic enzyme
| Gene name | pyk |
| Synonyms | pykA |
| Essential | no |
| Product | pyruvate kinase |
| Function | catabolic enzyme in glycolysis |
| MW, pI | 61,9 kDa, 4.88 |
| Gene length, protein length | 1755 bp, 585 amino acids |
| Immediate neighbours | pfkA, ytzA |
| Gene sequence (+200bp) | Protein sequence |
Genetic context 
| |
Contents
The gene
Basic information
- Coordinates: 2983830 - 2985584
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
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:ADP + phosphoenolpyruvate --> ATP + pyruvate, the reaction is irreversible under physiological conditions
- Protein family: pyruvate kinase family, (C-terminal section: PEP-utilizing enzyme family)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification: phosphorylation
- Cofactor(s): magnesium ion, potassium
- Effectors of protein activity:
- Interactions: Pyk-PfkA
- Localization: cytoplasm PubMed
Database entries
- Structure:
- Swiss prot entry: [3]
- KEGG entry: [4]
- E.C. number: [5]
Additional information
Expression and regulation
- Sigma factor:
- Regulation: twofold induced by glucose
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- Antibody:
Labs working on this gene/protein
Jörg Stülke, University of Göttingen, Germany Homepage
Your additional remarks
References
- Ludwig, H., Homuth, G., Schmalisch, M., Dyka, F. M., Hecker, M., and Stülke, J. (2001) Transcription of glycolytic genes and operons in Bacillus subtilis: evidence for the presence of multiple levels of control of the gapA operon. Mol Microbiol 41, 409-422.PubMed
- Jannière, L., Canceill, D., Suski, C., Kanga, S., Dalmais, B., Lestini, R., Monnier, A. F., Chapuis, J., Bolotin, A., Titok, M., Le Chatelier, E., and Ehrlich, S. D. (2007) Genetic evidence for a link between glycolysis and DNA replication. PLoS ONE 2, e447. PubMed
- Fry, B., Zhu, T., Domach, M. M., Koepsel, R. R., Phalakornkule, C., and Ataai, M. M. (2000) Characterization of growth and acid formation in a Bacillus subtilis pyruvate kinase mutant. Appl Env Microbiol 66: 4045-4049. PubMed
