iaaA:Quickview
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| Quickview | Gene | Gene Product(s) | Expression | Evolution | On One Page |
| References | Suggestions |
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| Standard Name |
iaaA |
|---|---|
| Gene Synonym(s) |
ECK0818, b0828, JW0812, spt, ybiK[1], ybiK |
| Product Desc. |
Component of asparaginase III α-β complex[3]; asparaginase III[3] isoAsp aminopeptidase, cleaves isoAsp-X dipeptides, Ntn hydrolase, weak L-asparaginase activity in vitro (EcAIII), precursor is cleaved into an alpha and beta subunit[4] heterotetrameric, glutathione utilization[5] |
| Product Synonyms(s) |
L-asparaginase[1], B0828[2][1], Spt[2][1], YbiK[2][1] , ECK0818, JW0812, spt, ybiK, b0828 |
| Function from GO |
<GO_nr /> |
| Knock-Out Phenotype | |
| Regulation/Expression | |
| Regulation/Activity | |
| Quick Links |
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Notes
E. coli IaaA is cleaved before Thr179 to expose an N-terminal nucleophile and to produce two subunits.[4] CysB regulon, sensitive to cysteine repression. The start of the Salmonella IaaA is confirmed by N-terminal sequencing of the IaaA precursor. Salmonella IaaA has been shown to have isoaspartyl-tripeptidase activity.[6] E. coli probably also has tripeptidase activity.[5] iaaA is a non-essential gene.[5]
References
- ↑ 1.0 1.1 1.2 1.3 1.4 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
- ↑ 2.0 2.1 2.2 2.3 2.4 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ 3.0 3.1 3.2 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ 4.0 4.1 Borek, D et al. (2004) Expression, purification and catalytic activity of Lupinus luteus asparagine beta-amidohydrolase and its Escherichia coli homolog. Eur. J. Biochem. 271 3215-26 PubMed
- ↑ 5.0 5.1 5.2 EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
- ↑ Larsen, RA et al. (2001) Aspartic peptide hydrolases in Salmonella enterica serovar typhimurium. J. Bacteriol. 183 3089-97 PubMed
