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Literature summary extracted from

  • Sungkeeree, P.; Toewiwat, N.; Whangsuk, W.; Ploypradith, P.; Mongkolsuk, S.; Loprasert, S.
    The esterase B from Sphingobium sp. SM42 has the new de-arenethiolase activity against cephalosporin antibiotics (2018), Biochem. Biophys. Res. Commun., 506, 231-236 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.1 gene estB, recombinant expression of His-tagged enzyme in Escherichia coli strain DH5alpha Sphingobium sp. SM42

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.1 Sphingobium sp. SM42 A0A0C5DFF8
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.1 recombinant His-tagged enzyme from Escherichia coli strain DH5alpha by nickel affinity chromatography Sphingobium sp. SM42

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.1 4-nitrophenyl acetate + H2O
-
 Sphingobium sp. SM42 4-nitrophenol + acetate
-
 ?
3.1.1.1 4-nitrophenyl butyrate + H2O
-
 Sphingobium sp. SM42 4-nitrophenol + butyrate
-
 ?
3.1.1.1 cefazolin + H2O 67% conversion Sphingobium sp. SM42 ?
-
 ?
3.1.1.1 cefoperazone + H2O 83% conversion Sphingobium sp. SM42 (2R)-2-[(4-ethyl-2,3-dioxopiperazinyl)carbonylamino]-2-(4-hydroxyphenyl)acetic acid + 1-methyl-1H-tetrazole-5-thiol + ?
-
 ?
3.1.1.1 cefotaxime + H2O 16% conversion Sphingobium sp. SM42 ?
-
 ?
3.1.1.1 ceftriaxone + H2O 18% conversion Sphingobium sp. SM42 ?
-
 ?
3.1.1.1 dibutyl phthalate + H2O
-
 Sphingobium sp. SM42 ?
-
 ?
3.1.1.1 additional information the enzyme EstB is active towards dibutyl phthalate, and can cleave some small aromatic ring side chains from cephalosporin derivatives. No activity against cephalosporin C and cefixime. EstB catalyzed the cleavage of the C-S bond found in cephalosporin derivatives to release the corresponding free aromatic ring side chains. EstB is active towards short-chain nitrophenyl esters (i.e. 4-nitrophenyl acetate (C2) and 4-nitrophenyl butyrate (C4)) and towards tributyrin. Substrate specificity of the Sphingobium sp. SM42 esteraseB (EstB) towards cephalosporin antibiotics Sphingobium sp. SM42 ?
-
 ?
3.1.1.1 tributyrin + H2O
-
 Sphingobium sp. SM42 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.1.1 ? x * 40000, about, sequence calculation Sphingobium sp. SM42

Synonyms

EC Number Synonyms Comment Organism
3.1.1.1 de-arenethiolase
-
 Sphingobium sp. SM42
3.1.1.1 EstB
-
 Sphingobium sp. SM42
3.1.1.1 esterase B
-
 Sphingobium sp. SM42

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.1.1.1 Sphingobium sp. SM42 sequence calculation
-
 5.3

General Information

EC Number General Information Comment Organism
3.1.1.1 physiological function esterase B from Sphingobium sp. SM42 exhibits de-arenethiolase activity against cephalosporin antibiotics. It is highly active against the third and first generation cephalosporins, cefoperazone and cefazolin and demonstrates a mild activity towards the third generation drugs, ceftriaxone and cefotaxime. The enzyme is one of two esterases whose genes have been isolated from the dibutyl phthalate (DBP)-degrading soil bacterium Sphingobium sp. SM42 Sphingobium sp. SM42