Three multidomain esterases from the cellulolytic rumen anaerobe Ruminococcus flavefaciens 17 that carry divergent dockerin sequences

V Aurilia, J C Martin, S I McCrae, K P Scott, M T Rincon, H J Flint

Research output: Contribution to journalArticle

65 Citations (Scopus)

Abstract

Three enzymes carrying esterase domains have been identified in the rumen cellulolytic anaerobe Ruminococcus flavefaciens 17, The newly characterized CesA gene product (768 amino acids) includes an N-terminal acetylesterase domain and an unidentified C-terminal domain, while the previously characterized XynB enzyme (781 amino acids) includes an internal acetylesterase domain in addition to its N-terminal xylanase catalytic domain. A third gene, xynE, is predicted to encode a multidomain enzyme of 792 amino acids including a family 11 xylanase domain and a C-terminal esterase domain. The esterase domains from CesA and XynB share significant sequence identity (44%) and belong to carbohydrate esterase family 3; both domains are shown here to be capable of deacetylating acetylated xylans, but no evidence was found for ferulic acid esterase activity. The esterase domain of XynE, however, shares 42 % amino acid identity with a family 1 phenolic acid esterase domain identified from Clostridum thermocellum XynZ, XynB, XynE and CesA all contain dockerin-like regions in addition to their catalytic domains, suggesting that these enzymes form part of a cellulosome-like multienzyme complex. The dockerin sequences of CesA and XynE differ significantly from those previously described in R, flavefaciens polysaccharidases, including XynB, suggesting that they might represent distinct dockerin specificities.

Original languageEnglish
Pages (from-to)1391-1397
Number of pages7
JournalMicrobiology
Volume146
Issue number6
Publication statusPublished - Jun 2000

Keywords

  • esterase
  • cellulosome
  • ruminococcus
  • rumen
  • dockerin
  • clostridium-thermocellum
  • cell-walls
  • acetyl xylan
  • P-coumaroyl
  • gene
  • family
  • domain
  • polysaccharides
  • identification
  • degradation

Cite this

Three multidomain esterases from the cellulolytic rumen anaerobe Ruminococcus flavefaciens 17 that carry divergent dockerin sequences. / Aurilia, V ; Martin, J C ; McCrae, S I ; Scott, K P ; Rincon, M T ; Flint, H J .

In: Microbiology , Vol. 146, No. 6, 06.2000, p. 1391-1397.

Research output: Contribution to journalArticle

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abstract = "Three enzymes carrying esterase domains have been identified in the rumen cellulolytic anaerobe Ruminococcus flavefaciens 17, The newly characterized CesA gene product (768 amino acids) includes an N-terminal acetylesterase domain and an unidentified C-terminal domain, while the previously characterized XynB enzyme (781 amino acids) includes an internal acetylesterase domain in addition to its N-terminal xylanase catalytic domain. A third gene, xynE, is predicted to encode a multidomain enzyme of 792 amino acids including a family 11 xylanase domain and a C-terminal esterase domain. The esterase domains from CesA and XynB share significant sequence identity (44{\%}) and belong to carbohydrate esterase family 3; both domains are shown here to be capable of deacetylating acetylated xylans, but no evidence was found for ferulic acid esterase activity. The esterase domain of XynE, however, shares 42 {\%} amino acid identity with a family 1 phenolic acid esterase domain identified from Clostridum thermocellum XynZ, XynB, XynE and CesA all contain dockerin-like regions in addition to their catalytic domains, suggesting that these enzymes form part of a cellulosome-like multienzyme complex. The dockerin sequences of CesA and XynE differ significantly from those previously described in R, flavefaciens polysaccharidases, including XynB, suggesting that they might represent distinct dockerin specificities.",
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AU - Scott, K P

AU - Rincon, M T

AU - Flint, H J

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N2 - Three enzymes carrying esterase domains have been identified in the rumen cellulolytic anaerobe Ruminococcus flavefaciens 17, The newly characterized CesA gene product (768 amino acids) includes an N-terminal acetylesterase domain and an unidentified C-terminal domain, while the previously characterized XynB enzyme (781 amino acids) includes an internal acetylesterase domain in addition to its N-terminal xylanase catalytic domain. A third gene, xynE, is predicted to encode a multidomain enzyme of 792 amino acids including a family 11 xylanase domain and a C-terminal esterase domain. The esterase domains from CesA and XynB share significant sequence identity (44%) and belong to carbohydrate esterase family 3; both domains are shown here to be capable of deacetylating acetylated xylans, but no evidence was found for ferulic acid esterase activity. The esterase domain of XynE, however, shares 42 % amino acid identity with a family 1 phenolic acid esterase domain identified from Clostridum thermocellum XynZ, XynB, XynE and CesA all contain dockerin-like regions in addition to their catalytic domains, suggesting that these enzymes form part of a cellulosome-like multienzyme complex. The dockerin sequences of CesA and XynE differ significantly from those previously described in R, flavefaciens polysaccharidases, including XynB, suggesting that they might represent distinct dockerin specificities.

AB - Three enzymes carrying esterase domains have been identified in the rumen cellulolytic anaerobe Ruminococcus flavefaciens 17, The newly characterized CesA gene product (768 amino acids) includes an N-terminal acetylesterase domain and an unidentified C-terminal domain, while the previously characterized XynB enzyme (781 amino acids) includes an internal acetylesterase domain in addition to its N-terminal xylanase catalytic domain. A third gene, xynE, is predicted to encode a multidomain enzyme of 792 amino acids including a family 11 xylanase domain and a C-terminal esterase domain. The esterase domains from CesA and XynB share significant sequence identity (44%) and belong to carbohydrate esterase family 3; both domains are shown here to be capable of deacetylating acetylated xylans, but no evidence was found for ferulic acid esterase activity. The esterase domain of XynE, however, shares 42 % amino acid identity with a family 1 phenolic acid esterase domain identified from Clostridum thermocellum XynZ, XynB, XynE and CesA all contain dockerin-like regions in addition to their catalytic domains, suggesting that these enzymes form part of a cellulosome-like multienzyme complex. The dockerin sequences of CesA and XynE differ significantly from those previously described in R, flavefaciens polysaccharidases, including XynB, suggesting that they might represent distinct dockerin specificities.

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KW - clostridium-thermocellum

KW - cell-walls

KW - acetyl xylan

KW - P-coumaroyl

KW - gene

KW - family

KW - domain

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KW - identification

KW - degradation

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