Analysis of the structure and substrate scope of chitooligosaccharide oxidase reveals high affinity for C2-modified glucosamines
© 2020 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies..
Chitooligosaccharide oxidase (ChitO) is a fungal carbohydrate oxidase containing a bicovalently bound FAD cofactor. The enzyme is known to catalyse the oxidation of chitooligosaccharides, oligomers of N-acetylated glucosamines derived from chitin degradation. In this study, the unique substrate acceptance was explored by testing a range of N-acetyl-d-glucosamine derivatives, revealing that ChitO preferentially accepts carbohydrates with a hydrophobic group attached to C2. The enzyme also accepts streptozotocin, a natural product used to treat tumours. Elucidation of the crystal structure provides an explanation for the high affinity towards C2-decorated glucosamines: the active site has a secondary binding pocket that accommodates groups attached at C2. Docking simulations are fully in line with the observed substrate preference. This work expands the knowledge on this versatile enzyme.
| Medienart: |
E-Artikel |
|---|
| Erscheinungsjahr: |
2020 |
|---|---|
| Erschienen: |
2020 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:594 |
|---|---|
| Enthalten in: |
FEBS letters - 594(2020), 17 vom: 01. Sept., Seite 2819-2828 |
| Sprache: |
Englisch |
|---|
| Beteiligte Personen: |
Savino, Simone [VerfasserIn] |
|---|
| Links: |
|---|
| Anmerkungen: |
Date Completed 13.05.2021 Date Revised 04.12.2021 published: Print-Electronic Citation Status MEDLINE |
|---|
| doi: |
10.1002/1873-3468.13854 |
|---|
| funding: |
|
|---|---|
| Förderinstitution / Projekttitel: |
|
| PPN (Katalog-ID): |
NLM310713811 |
|---|
| LEADER | 01000naa a22002652 4500 | ||
|---|---|---|---|
| 001 | NLM310713811 | ||
| 003 | DE-627 | ||
| 005 | 20231225140702.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 231225s2020 xx |||||o 00| ||eng c | ||
| 024 | 7 | |a 10.1002/1873-3468.13854 |2 doi | |
| 028 | 5 | 2 | |a pubmed24n1035.xml |
| 035 | |a (DE-627)NLM310713811 | ||
| 035 | |a (NLM)32491191 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 100 | 1 | |a Savino, Simone |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Analysis of the structure and substrate scope of chitooligosaccharide oxidase reveals high affinity for C2-modified glucosamines |
| 264 | 1 | |c 2020 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a ƒaComputermedien |b c |2 rdamedia | ||
| 338 | |a ƒa Online-Ressource |b cr |2 rdacarrier | ||
| 500 | |a Date Completed 13.05.2021 | ||
| 500 | |a Date Revised 04.12.2021 | ||
| 500 | |a published: Print-Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a © 2020 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies. | ||
| 520 | |a Chitooligosaccharide oxidase (ChitO) is a fungal carbohydrate oxidase containing a bicovalently bound FAD cofactor. The enzyme is known to catalyse the oxidation of chitooligosaccharides, oligomers of N-acetylated glucosamines derived from chitin degradation. In this study, the unique substrate acceptance was explored by testing a range of N-acetyl-d-glucosamine derivatives, revealing that ChitO preferentially accepts carbohydrates with a hydrophobic group attached to C2. The enzyme also accepts streptozotocin, a natural product used to treat tumours. Elucidation of the crystal structure provides an explanation for the high affinity towards C2-decorated glucosamines: the active site has a secondary binding pocket that accommodates groups attached at C2. Docking simulations are fully in line with the observed substrate preference. This work expands the knowledge on this versatile enzyme | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a chitooligosaccharides | |
| 650 | 4 | |a covalent flavin | |
| 650 | 4 | |a crystal structure | |
| 650 | 4 | |a glucosamine | |
| 650 | 4 | |a oxidation | |
| 650 | 7 | |a Fungal Proteins |2 NLM | |
| 650 | 7 | |a Oligosaccharides |2 NLM | |
| 650 | 7 | |a Recombinant Proteins |2 NLM | |
| 650 | 7 | |a oligochitosan |2 NLM | |
| 650 | 7 | |a Chitin |2 NLM | |
| 650 | 7 | |a 1398-61-4 |2 NLM | |
| 650 | 7 | |a Flavin-Adenine Dinucleotide |2 NLM | |
| 650 | 7 | |a 146-14-5 |2 NLM | |
| 650 | 7 | |a Chitosan |2 NLM | |
| 650 | 7 | |a 9012-76-4 |2 NLM | |
| 650 | 7 | |a Oxidoreductases |2 NLM | |
| 650 | 7 | |a EC 1.- |2 NLM | |
| 650 | 7 | |a Glucosamine |2 NLM | |
| 650 | 7 | |a N08U5BOQ1K |2 NLM | |
| 700 | 1 | |a Jensen, Sonja |e verfasserin |4 aut | |
| 700 | 1 | |a Terwisscha van Scheltinga, Anke |e verfasserin |4 aut | |
| 700 | 1 | |a Fraaije, Marco W |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t FEBS letters |d 1968 |g 594(2020), 17 vom: 01. Sept., Seite 2819-2828 |w (DE-627)NLM000016691 |x 1873-3468 |7 nnns |
| 773 | 1 | 8 | |g volume:594 |g year:2020 |g number:17 |g day:01 |g month:09 |g pages:2819-2828 |
| 856 | 4 | 0 | |u http://dx.doi.org/10.1002/1873-3468.13854 |3 Volltext |
| 912 | |a GBV_USEFLAG_A | ||
| 912 | |a GBV_NLM | ||
| 951 | |a AR | ||
| 952 | |d 594 |j 2020 |e 17 |b 01 |c 09 |h 2819-2828 | ||