Glucuronan lyases from family PL7 use a Tyr/Tyr syn β-elimination catalytic mechanism for glucuronan breakdown

Marlene Vuillemin; Bo Pilgaard; Emma Kiehn; Folmer Fredslund; Ditte H. Welner; Anne S. Meyer; Finn L. Aachmann; Casper Wilkens

doi:10.1039/d3cc04256a

Glucuronan lyases from family PL7 use a Tyr/Tyr syn β-elimination catalytic mechanism for glucuronan breakdown

Marlene Vuillemin, Bo Pilgaard, Emma Kiehn, Folmer Fredslund, Ditte H. Welner, Anne S. Meyer, Finn L. Aachmann, Casper Wilkens^*

^*Corresponding author for this work

Norwegian University of Science and Technology

Research output: Contribution to journal › Journal article › Research › peer-review

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Abstract

TpPL7A and TpPL7B, members of CAZy family PL7, act as β-glucuronan lyases. TpPL7A diverges by lacking the catalytic histidine, identified as the Brønsted base in PL7 alginate lyases. Our research, including TpPL7A's crystal structure, and mutagenesis studies, reveals a shared syn-β-elimination mechanism with a single tyrosine serving as both base and acid catalyst. This mechanism may extend to subfamily PL7_4 glucuronan lyases.

Original language	English
Journal	Chemical Communications
Volume	60
Issue number	4
Pages (from-to)	440-443
Number of pages	4
ISSN	1359-7345
DOIs	https://doi.org/10.1039/d3cc04256a
Publication status	Published - 2024

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@article{8c0102a9fa754783bd797f54dc698473,

title = "Glucuronan lyases from family PL7 use a Tyr/Tyr syn β-elimination catalytic mechanism for glucuronan breakdown",

abstract = "TpPL7A and TpPL7B, members of CAZy family PL7, act as β-glucuronan lyases. TpPL7A diverges by lacking the catalytic histidine, identified as the Br{\o}nsted base in PL7 alginate lyases. Our research, including TpPL7A's crystal structure, and mutagenesis studies, reveals a shared syn-β-elimination mechanism with a single tyrosine serving as both base and acid catalyst. This mechanism may extend to subfamily PL7_4 glucuronan lyases.",

author = "Marlene Vuillemin and Bo Pilgaard and Emma Kiehn and Folmer Fredslund and Welner, {Ditte H.} and Meyer, {Anne S.} and Aachmann, {Finn L.} and Casper Wilkens",

year = "2024",

doi = "10.1039/d3cc04256a",

language = "English",

volume = "60",

pages = "440--443",

journal = "Chemical Communications",

issn = "1359-7345",

publisher = "Royal Society of Chemistry",

number = "4",

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TY - JOUR

T1 - Glucuronan lyases from family PL7 use a Tyr/Tyr syn β-elimination catalytic mechanism for glucuronan breakdown

AU - Vuillemin, Marlene

AU - Pilgaard, Bo

AU - Kiehn, Emma

AU - Fredslund, Folmer

AU - Welner, Ditte H.

AU - Meyer, Anne S.

AU - Aachmann, Finn L.

AU - Wilkens, Casper

PY - 2024

Y1 - 2024

N2 - TpPL7A and TpPL7B, members of CAZy family PL7, act as β-glucuronan lyases. TpPL7A diverges by lacking the catalytic histidine, identified as the Brønsted base in PL7 alginate lyases. Our research, including TpPL7A's crystal structure, and mutagenesis studies, reveals a shared syn-β-elimination mechanism with a single tyrosine serving as both base and acid catalyst. This mechanism may extend to subfamily PL7_4 glucuronan lyases.

AB - TpPL7A and TpPL7B, members of CAZy family PL7, act as β-glucuronan lyases. TpPL7A diverges by lacking the catalytic histidine, identified as the Brønsted base in PL7 alginate lyases. Our research, including TpPL7A's crystal structure, and mutagenesis studies, reveals a shared syn-β-elimination mechanism with a single tyrosine serving as both base and acid catalyst. This mechanism may extend to subfamily PL7_4 glucuronan lyases.

U2 - 10.1039/d3cc04256a

DO - 10.1039/d3cc04256a

M3 - Journal article

C2 - 38087900

SN - 1359-7345

VL - 60

SP - 440

EP - 443

JO - Chemical Communications

JF - Chemical Communications

IS - 4

ER -

Glucuronan lyases from family PL7 use a Tyr/Tyr syn β-elimination catalytic mechanism for glucuronan breakdown

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