Esterase EstB
Details
- Name
- Esterase EstB
- Synonyms
- 3.1.1.-
- Gene Name
- estB
- Organism
- Pseudomonas marginata
- Amino acid sequence
>lcl|BSEQ0017055|Esterase EstB MTAASLDPTAFSLDAASLAARLDAVFDQALRERRLVGAVAIVARHGEILYRRAQGLADRE AGRPMREDTLFRLASVTKPIVALAVLRLVARGELALDAPVTRWLPEFRPRLADGSEPLVT IHHLLTHTSGLGYWLLEGAGSVYDRLGISDGIDLRDFDLDENLRRLASAPLSFAPGSGWQ YSLALDVLGAVVERATGQPLAAAVDALVAQPLGMRDCGFVSAEPERFAVPYHDGQPEPVR MRDGIEVPLPEGHGAAVRFAPSRVFEPGAYPSGGAGMYGSADDVLRALEAIRANPGFLPE TLADAARRDQAGVGAETRGPGWGFGYLSAVLDDPAAAGTPQHAGTLQWGGVYGHSWFVDR ALGLSVLLLTNTAYEGMSGPLTIALRDAVYAR
- Number of residues
- 392
- Molecular Weight
- 41706.785
- Theoretical pI
- 5.12
- GO Classification
- Functionshydrolase activityComponentscytoplasm
- General Function
- Hydrolase activity
- Specific Function
- Acts on short-chain (C4-C6) fatty acid esters and triglycerides, including tertiary alcohol esters. Activity on p-nitrophenyl esters is generally higher than on o-nitrophenyl esters. Lacks beta-lactamase activity; it hydrolyzes the ester bond of cephalosporin substrates but there is no opening of the beta-lactam ring observed.
- Pfam Domain Function
- Beta-lactamase (PF00144)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0006446|1179 bp TCAGCGCGCGTAGACGGCGTCGCGCAAGGCGATCGTCAGCGGGCCCGACATGCCTTCGTA GGCGGTATTGGTGAGCAGCAGCACGCTGAGTCCCAGCGCGCGGTCGACGAACCAGGAATG GCCATAGACGCCGCCCCATTGCAGCGTCCCGGCGTGCTGCGGGGTGCCGGCCGCGGCCGG ATCGTCGAGCACCGCGCTCAGGTAGCCGAAGCCCCAGCCGGGGCCGCGCGTCTCGGCGCC GACTCCGGCCTGGTCGCGGCGCGCCGCGTCGGCCAGCGTCTCGGGCAGGAAACCGGGATT GGCGCGGATCGCCTCGAGCGCGCGCAGGACGTCGTCGGCCGAGCCGTACATGCCGGCGCC GCCCGAGGGATAGGCGCCCGGCTCGAACACGCGGGAGGGCGCGAAACGCACGGCCGCGCC GTGGCCTTCCGGCAGCGGCACCTCGATGCCGTCGCGCATGCGCACCGGCTCCGGCTGGCC GTCGTGGTAAGGCACGGCGAAGCGCTCGGGCTCCGCCGAGACGAAACCGCAATCGCGCAT GCCGAGCGGCTGGGCGACCAACGCGTCCACCGCCGCGGCCAGCGGCTGCCCGGTGGCGCG CTCGACCACCGCGCCGAGCACGTCGAGCGCCAGCGAATACTGCCAGCCGCTGCCCGGCGC GAAGGACAGCGGCGCCGAGGCGAGGCGGCGCAGGTTTTCGTCGAGATCGAAGTCGCGCAG GTCGATGCCGTCCGAGATGCCGAGCCGGTCGTACACGGAGCCGGCGCCCTCGAGCAGCCA GTAGCCGAGCCCCGACGTGTGCGTGAGCAGGTGGTGAATCGTGACGAGCGGCTCGCTGCC GTCGGCCAGCCGCGGCCGGAATTCGGGCAACCAGCGCGTGACCGGCGCGTCGAGCGCGAG TTCGCCGCGCGCCACCAGCCGCAGCACCGCCAGCGCGACGATCGGCTTGGTCACCGAAGC GAGCCGGAACAGCGTGTCCTCGCGCATCGGCCGACCTGCCTCTCGGTCGGCCAGGCCCTG GGCGCGGCGATACAGGATCTCGCCGTGCCGCGCGACGATCGCCACCGCGCCGACCAGGCG CCGTTCGCGCAGCGCCTGGTCGAACACGGCATCGAGACGCGCGGCCAGCGAGGCGGCATC GAGGGAGAAAGCGGTCGGGTCGAGCGAGGCAGCGGTCAT
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q9KX40 UniProtKB Entry Name ESTB_BURGA GenBank Gene ID U33634 - General References
- Petersen EI, Valinger G, Solkner B, Stubenrauch G, Schwab H: A novel esterase from Burkholderia gladioli which shows high deacetylation activity on cephalosporins is related to beta-lactamases and DD-peptidases. J Biotechnol. 2001 Jul 26;89(1):11-25. [Article]
- Valinger G, Hermann M, Wagner UG, Schwab H: Stability and activity improvement of cephalosporin esterase EstB from Burkholderia gladioli by directed evolution and structural interpretation of muteins. J Biotechnol. 2007 Mar 30;129(1):98-108. Epub 2006 Oct 20. [Article]
- Ivancic M, Valinger G, Gruber K, Schwab H: Inverting enantioselectivity of Burkholderia gladioli esterase EstB by directed and designed evolution. J Biotechnol. 2007 Mar 30;129(1):109-22. Epub 2006 Oct 20. [Article]
- Wagner UG, Petersen EI, Schwab H, Kratky C: EstB from Burkholderia gladioli: a novel esterase with a beta-lactamase fold reveals steric factors to discriminate between esterolytic and beta-lactam cleaving activity. Protein Sci. 2002 Mar;11(3):467-78. [Article]