CA2427029A1 - Variants of soluble pyrroloquinoline quinone-dependent glucose dehydrogenase - Google Patents
Variants of soluble pyrroloquinoline quinone-dependent glucose dehydrogenase Download PDFInfo
- Publication number
- CA2427029A1 CA2427029A1 CA002427029A CA2427029A CA2427029A1 CA 2427029 A1 CA2427029 A1 CA 2427029A1 CA 002427029 A CA002427029 A CA 002427029A CA 2427029 A CA2427029 A CA 2427029A CA 2427029 A1 CA2427029 A1 CA 2427029A1
- Authority
- CA
- Canada
- Prior art keywords
- gdh
- amino acid
- mutant
- further characterized
- pqq
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
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Classifications
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0006—Oxidoreductases (1.) acting on CH-OH groups as donors (1.1)
Abstract
The present invention relates to improved variants of soluble pyrroloquinoli ne quinone (PQQ)-dependent glucose dehydrogenases (s-GDH), to genes encoding mutated s-GDH, to mutant proteins of s-GDH with improved substrate specifici ty for glucose, and to different applications of these s-GDH variants, particularly for determining concentrations of sugar, especially of glucose in a sample.
Claims (30)
1. A mutant of the soluble form of EC 1.1.99.17 also known as PQQ-dependent soluble glucose dehydrogenase (s-GDH) said mutant characterized in that relative to the corresponding wild-type enzyme and with regard to at least one other selected sugar substrate, it has an at least two-fold increased substrate specificity for glucose.
2. The mutant according to claim 1 further characterized in that said selected sugar is selected from the group consisting of maltose and galactose.
3. The mutant according to claim 1 or 2 further characterized in that said selected sugar is maltose.
4. The mutant of PQQ-dependent s-GDH according to Claim 1 further characterized in that said substrate specificity for glucose is improved at least 3-fold.
5. The mutant of PQQ-dependent s-GDH according to Claim 1 further characterized in that said substrate specificity for glucose is improved at least 5-fold.
6. A mutant of the soluble form of EC 1.1.99.17 also known as PQQ-dependent soluble glucose dehydrogenase (s-GDH) said mutant characterized in that a) the substrate specific reactivity towards glucose is essentially equal to that of the wild-type enzyme, and b) the substrate specific reactivity towards maltose is 30% or less as compared to the wild-type enzyme.
7. The mutant according to claim 6 further characterized in that said substrate specific reactivity towards maltose is 20% or less as compared to the wild-type enzyme.
8. The mutant of a PQQ-dependent s-GDH according to any of claims 1- 7 further characterized in that the wild-type s-GDH is isolated from a strain of the Acineto-bacter species group consisting of A, calcoaceticus and A. baumannii.
9. A mutant protein of PQQ-dependent s-GDH comprising an amino acid residue substitution at the amino acid position corresponding to position 348 of the s-GDH
wild-type sequence known from A. calcoaceticus (SEQ ID NO: 24).
wild-type sequence known from A. calcoaceticus (SEQ ID NO: 24).
10. A mutant protein of PQQ-dependent s-GDH comprising at least two amino acid residue substitutions at amino acid positions corresponding to positions of the s-GDH wild-type sequence known from A. calcoaceticus (SEQ ID NO: 24), said sub-stituted amino acid positions being selected from the group consisting of positions 16, 22, 76, 116, 120 ,127, 143, 168, 169, 171, 177, 227, 230, 231, 245, 255, 277, 295, 299, 308, 317, 341, 349, 355, 422, 428 and 438, wherein the amino acid residue T348 is replaced.
11. The mutant of claim 10 further characterized in that at amino acid positions corre-sponding to positions of the s-GDH wild-type sequence known from A.
calcoaceticus (SEQ ID NO: 24) the amino acid in position 348 and at least one of the following amino acid residues 16, 116, 120, 127, 169, 171, 177, 227, 255, 277, 299, 317, 355 and 438 are substituted.
calcoaceticus (SEQ ID NO: 24) the amino acid in position 348 and at least one of the following amino acid residues 16, 116, 120, 127, 169, 171, 177, 227, 255, 277, 299, 317, 355 and 438 are substituted.
12. The mutant protein of claim 10 comprising substitutions of the amino acid residues at positions 348 and 428.
13. A mutant protein of PQQ-dependent s-GDH comprising at least three amino acid residue substitutions at amino acid positions corresponding positions of the s-GDH
wild-type sequence known from A. calcoaceticus (SEQ ID NO: 24), said substituted amino acid positions being selected from the group consisting of positions 171, 227, 230, 245, 341, 348, 349, and 428 wherein both the amino acid residues T348 and N428 are substituted.
wild-type sequence known from A. calcoaceticus (SEQ ID NO: 24), said substituted amino acid positions being selected from the group consisting of positions 171, 227, 230, 245, 341, 348, 349, and 428 wherein both the amino acid residues T348 and N428 are substituted.
14. The mutant according to claim 12 or 13 further characterized in that asparagine at position 428 is substituted with an amino acid residue selected from the group con-sisting of leucine, proline and valine.
15. The mutant according to any of claims 9 to 14 further characterized in that threo-nine at position 348 is substituted with an amino acid residue selected from the group consisting of alanine, glycine and serine.
16. A mutant protein of PQQ-dependent s-GDH comprising the amino acid sequence of WPXaaVAPS (SEQ ID NO: 1), wherein said Xaa residue is an amino acid residue other than threonine.
17. The mutant protein of claim 16 further characterized in that said Xaa residue is gly-cine.
18. A mutant protein of PQQ-dependent s-GDH comprising the amino acid sequence of TAGXaaVQK (SEQ ID NO: 2), wherein said Xaa residue is an amino acid residue other than asparagine.
19. The mutant protein of claim 18 further characterized in that said Xaa residue is pro-line.
20. A mutant protein of PQQ-dependent s-GDH comprising the amino acid sequence of ADGXaaNGL (SEQ ID NO: 3), wherein said Xaa residue is an amino acid residue other than glutamine.
21. The mutant of claim 20 further characterized in that said Xaa residue is selected from the group consisting of aspartic acid, glutamic acid, methionine, proline, ser-ine, alanine or glycine.
22. An isolated polynucleotide encoding the s-GDH mutant protein according to any of claims 9 to 21.
23. An expression vector comprising an isolated polynucleotide as defined in claim 22 operably linked to a promoter sequence capable of promoting the expression of said polynucleotide in a host cell.
24. A host cell comprising the expression vector of claim 23.
25. A process for producing s-GDH variants comprising culturing the host cell of claim 24 under conditions suitable for production of the enzyme variants.
26. An expression vector comprising an isolated polynucleotide as defined in claim 22 operably linked to a promoter sequence capable of promoting its expression in a cell-free peptide synthesis system.
27. A process for producing s-GDH variants with the construct of claim 26 in a cell-free peptide synthesis system under conditions suitable for production of the said en-zyme variants.
28. A method of detecting, determining or measuring glucose in a sample using a s-GDH mutant according to any of the preceeding claims, said improvement com-prising contacting the sample with the mutant.
29. The method of claim 28 further characterized in that said detection, determination or measurement of glucose is performed using a sensor or test strip device.
30. A device for the detection or measurement of glucose in a sample comprising a s-GDH mutant according to any of claims 1-29 and other reagents required for said measurement.
Applications Claiming Priority (5)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
EP00123512.6 | 2000-10-27 | ||
EP00123512 | 2000-10-27 | ||
EP00127294.7 | 2000-12-19 | ||
EP00127294 | 2000-12-19 | ||
PCT/EP2001/012148 WO2002034919A1 (en) | 2000-10-27 | 2001-10-20 | Variants of soluble pyrroloquinoline quinone-dependent glucose dehydrogenase |
Publications (2)
Publication Number | Publication Date |
---|---|
CA2427029A1 true CA2427029A1 (en) | 2002-05-02 |
CA2427029C CA2427029C (en) | 2010-02-02 |
Family
ID=26071553
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
CA002427029A Expired - Lifetime CA2427029C (en) | 2000-10-27 | 2001-10-20 | Variants of soluble pyrroloquinoline quinone-dependent glucose dehydrogenase |
Country Status (12)
Country | Link |
---|---|
US (3) | US20030104595A1 (en) |
EP (1) | EP1332216B1 (en) |
JP (2) | JP3845618B2 (en) |
KR (1) | KR100519902B1 (en) |
CN (1) | CN1288246C (en) |
AT (1) | ATE520777T1 (en) |
AU (2) | AU2002215966B2 (en) |
BR (1) | BRPI0114962B8 (en) |
CA (1) | CA2427029C (en) |
HK (1) | HK1074217A1 (en) |
PL (1) | PL205561B1 (en) |
WO (1) | WO2002034919A1 (en) |
Families Citing this family (45)
Publication number | Priority date | Publication date | Assignee | Title |
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WO2001059080A1 (en) * | 2000-02-11 | 2001-08-16 | Millennium Pharmaceuticals, Inc. | 18477, a human protein kinase and uses therefor |
CA2427029C (en) * | 2000-10-27 | 2010-02-02 | F. Hoffmann-La Roche Ag | Variants of soluble pyrroloquinoline quinone-dependent glucose dehydrogenase |
JP2003093071A (en) * | 2001-09-26 | 2003-04-02 | Koji Hayade | Glucose dehydrogenase |
US6855556B2 (en) * | 2002-01-04 | 2005-02-15 | Becton, Dickinson And Company | Binding protein as biosensors |
US7476525B2 (en) | 2002-05-27 | 2009-01-13 | Toyo Boseki Kabushiki Kaisha | Modified pyrroloquinoline quinone (PQQ) dependent glucose dehydrogenase with superior substrate specificity and stability |
DE60323650D1 (en) | 2002-07-04 | 2008-10-30 | Ultizyme Int Ltd | glucose dehydrogenase |
AU2003299104A1 (en) | 2002-09-27 | 2004-04-19 | Dsm Ip Assets B.V. | Aldehyde dehydrogenase gene |
CA2511656A1 (en) * | 2002-12-24 | 2004-07-15 | Ikeda Food Research Co., Ltd. | Coenzyme-binding glucose dehydrogenase |
JP4415282B2 (en) * | 2003-03-24 | 2010-02-17 | 東洋紡績株式会社 | Modified pyrroloquinoline quinone (PQQ) -dependent glucose dehydrogenase excellent in substrate specificity or stability |
DE10320259A1 (en) * | 2003-05-07 | 2004-11-25 | Bayer Technology Services Gmbh | Novel glucose dehydrogenase and its production |
US7479383B2 (en) | 2003-09-08 | 2009-01-20 | Toyo Boseki Kabushiki Kaisha | Modified pyrroloquinoline quinone (PQQ) dependent glucose dehydrogenase excellent in substrate specificity |
JP2005328793A (en) * | 2004-05-21 | 2005-12-02 | Toyobo Co Ltd | Pyrroloquinoline quinone (pqq)-dependent glucose dehydrogenase modifier excellent in substrate specificity |
EP1600503A1 (en) * | 2004-05-14 | 2005-11-30 | Amano Enzyme Inc. | Modified pyrroloquinoline quinone-dependent glucose dehydrogenase |
US7037698B2 (en) | 2004-05-19 | 2006-05-02 | Amano Enzyme Inc. | Pyrroloquinoline quinone-dependent glucose dehydrogenase |
US20060003400A1 (en) * | 2004-06-30 | 2006-01-05 | Byrd Patricia A | Methods and compositions for characterizing a redox reagent system enzyme |
BRPI0513691A (en) * | 2004-07-20 | 2008-03-25 | Roche Diagnostics Gmbh | genetically transformed pyrroloquinoline-dependent quinone-dependent glucose dehydrogenase comprising an amino acid insert |
ES2537106T3 (en) | 2004-10-15 | 2015-06-02 | F. Hoffmann-La Roche Ag | Thermostable mutants of the quinone-dependent glucose dehydrogenase of pyrroloquinoline |
US7901921B2 (en) * | 2004-10-22 | 2011-03-08 | Oncolytics Biotech Inc. | Viral purification methods |
WO2006085509A1 (en) * | 2005-02-08 | 2006-08-17 | Toyo Boseki Kabushiki Kaisha | Modified pyrroloquinolinequinone-dependent glucose dehydrogenase having excellent substrate-specificity |
EP2365073A1 (en) | 2005-03-25 | 2011-09-14 | Ikeda Food Research Co. Ltd. | Coenzyme-linked glucose dehydrogenase and polynucleotide encoding the same |
WO2006109578A1 (en) * | 2005-04-05 | 2006-10-19 | Amano Enzyme Inc. | Altered pyrroloquinoline-quinone-dependent glucose dehydrogenase and method of improving substrate specificity of pyrroloquinoline-quinone-dependent glucose dehydrogenase |
ATE455848T1 (en) * | 2005-06-20 | 2010-02-15 | Arkray Inc | MUTANT GLUCOSE DEHYDROGENASE |
TW200706650A (en) * | 2005-08-11 | 2007-02-16 | Toyo Boseki | A substrate specificity improved composition for glucose measurement |
JP2007043984A (en) * | 2005-08-11 | 2007-02-22 | Toyobo Co Ltd | Method for improving substrate specificity of pyrroloquinoline quinone dependent glucose dehydrogenase |
US7955484B2 (en) | 2005-12-14 | 2011-06-07 | Nova Biomedical Corporation | Glucose biosensor and method |
PT2010649T (en) | 2006-04-13 | 2017-05-03 | Hoffmann La Roche | Improved mutants of pyrroloquinoline quinone dependent soluble glucose dehydrogenase |
KR100973992B1 (en) * | 2006-05-25 | 2010-08-05 | 삼성전자주식회사 | Apparatus for tdd switching in tdd wireless communication system |
JP4665235B2 (en) | 2006-06-29 | 2011-04-06 | 池田食研株式会社 | FAD-linked glucose dehydrogenase gene |
US8619038B2 (en) * | 2007-09-04 | 2013-12-31 | Apple Inc. | Editing interface |
DE102008030435A1 (en) * | 2008-06-26 | 2010-01-07 | Bayer Technology Services Gmbh | Novel variants of PQQ-dependent glucose hydrogenase with improved substrate specificity |
FR2948680B1 (en) * | 2009-07-28 | 2013-10-04 | Centre Nat Rech Scient | NEW MUTANTS OF THE PQQ S-GDH |
US20130092536A1 (en) | 2010-07-23 | 2013-04-18 | Roche Diagnostics Operations, Inc. | Zwitterion buffer containing compositions and uses in electroanalytical methods |
EP2465936A1 (en) | 2010-12-20 | 2012-06-20 | LEK Pharmaceuticals d.d. | Enzymatic synthesis of statins and intermediates thereof |
JP6194251B2 (en) | 2010-12-20 | 2017-09-06 | レツク・フアーマシユーテイカルズ・デー・デー | Enzymatic synthesis of active pharmaceutical ingredients and their intermediates |
EP2656058A1 (en) | 2010-12-22 | 2013-10-30 | Roche Diagnostics GmbH | Systems and methods to compensate for sources of error during electrochemical testing |
CN102559624B (en) * | 2012-03-05 | 2013-10-16 | 浙江德清汇宁生物科技有限公司 | Thermostable mutant of pyrroloquiniline quinine-dependent glucose dehydrogenase and high-throughput screening method thereof |
EP2636750A1 (en) | 2012-03-06 | 2013-09-11 | Roche Diagniostics GmbH | Compatible solute ectoine as well as derivatives thereof for enzyme stabilization |
EP2994536B1 (en) | 2013-05-08 | 2017-06-14 | Roche Diabetes Care GmbH | Stabilization of enzymes by nicotinic acid |
EP3074524B1 (en) | 2013-11-27 | 2019-11-06 | Roche Diabetes Care GmbH | Composition comprising up-converting phosphors for detecting an analyte |
EP2927319A1 (en) | 2014-03-31 | 2015-10-07 | Roche Diagnostics GmbH | High load enzyme immobilization by crosslinking |
EP3131882B1 (en) | 2014-04-14 | 2020-07-15 | Roche Diagnostics GmbH | Phenazinium mediators |
US10060907B2 (en) | 2014-08-22 | 2018-08-28 | Roche Diagnostic Operations, Inc. | Redoxindicators |
CN105331591B (en) * | 2015-10-29 | 2020-02-28 | 英科隆生物技术(杭州)有限公司 | PQQ-sGDH mutant, polynucleotide and glucose detection device |
EP3523639A4 (en) | 2016-10-05 | 2020-06-03 | H. Hoffnabb-La Roche Ag | Detection reagents and electrode arrangements for multi-analyte diagnostic test elements, as well as methods of using the same |
CN113234697B (en) * | 2021-04-28 | 2022-09-02 | 遵义医科大学珠海校区 | Glucose dehydrogenase variant and preparation method and application thereof |
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DE3716957A1 (en) | 1987-05-20 | 1988-12-01 | Boehringer Mannheim Gmbh | EXPRESSION VECTOR FOR ADJUSTABLE EXPRESSION OF FOREIGN GENES IN PROKARYONTS |
US6190906B1 (en) | 1987-05-20 | 2001-02-20 | Roche Diagnostics Gmbh | Expression vector for the regulatable expression of foreign genes in prokaryotes |
FI905324A (en) | 1990-10-29 | 1992-04-30 | Valtion Teknillinen | ENZYMATISKT BESTAEMNINGSFOERFARANDE FOER ALDOSER. |
DE4311464A1 (en) | 1993-04-08 | 1994-10-13 | Boehringer Mannheim Gmbh | Method for the colorimetric determination of an analyte with a PQQ-dependent dehydrogenase |
DE19639169A1 (en) * | 1996-09-24 | 1998-04-02 | Boehringer Mannheim Gmbh | Redox-active compounds and their application |
JPH10243786A (en) * | 1997-03-03 | 1998-09-14 | Koji Hayade | Modified glucose dehydrogenase |
CZ291059B6 (en) * | 1997-03-12 | 2002-12-11 | Lonza Ag | Process for preparing esters of 2,6-pyridinedicarboxylic acids |
US5997817A (en) | 1997-12-05 | 1999-12-07 | Roche Diagnostics Corporation | Electrochemical biosensor test strip |
JP2000350588A (en) * | 1999-04-08 | 2000-12-19 | Koji Hayade | Glucose dehydrogenase |
TWI224136B (en) * | 1999-04-30 | 2004-11-21 | Koji Sode | Glucose dehydrogenase |
CA2427029C (en) * | 2000-10-27 | 2010-02-02 | F. Hoffmann-La Roche Ag | Variants of soluble pyrroloquinoline quinone-dependent glucose dehydrogenase |
JP2003093071A (en) | 2001-09-26 | 2003-04-02 | Koji Hayade | Glucose dehydrogenase |
-
2001
- 2001-10-20 CA CA002427029A patent/CA2427029C/en not_active Expired - Lifetime
- 2001-10-20 KR KR10-2003-7005783A patent/KR100519902B1/en active IP Right Grant
- 2001-10-20 JP JP2002537889A patent/JP3845618B2/en not_active Expired - Lifetime
- 2001-10-20 PL PL362548A patent/PL205561B1/en unknown
- 2001-10-20 WO PCT/EP2001/012148 patent/WO2002034919A1/en active IP Right Grant
- 2001-10-20 AT AT01988775T patent/ATE520777T1/en not_active IP Right Cessation
- 2001-10-20 AU AU2002215966A patent/AU2002215966B2/en not_active Expired
- 2001-10-20 EP EP01988775A patent/EP1332216B1/en not_active Expired - Lifetime
- 2001-10-20 AU AU1596602A patent/AU1596602A/en active Pending
- 2001-10-20 BR BRPI0114962A patent/BRPI0114962B8/en not_active IP Right Cessation
- 2001-10-20 CN CNB018212158A patent/CN1288246C/en not_active Expired - Lifetime
- 2001-10-29 US US10/082,627 patent/US20030104595A1/en not_active Abandoned
-
2002
- 2002-12-13 US US10/319,147 patent/US7132270B2/en not_active Expired - Lifetime
-
2005
- 2005-08-02 HK HK05106631A patent/HK1074217A1/en not_active IP Right Cessation
- 2005-12-09 US US11/298,778 patent/US7547535B2/en not_active Expired - Fee Related
-
2006
- 2006-06-05 JP JP2006156710A patent/JP3889434B2/en not_active Expired - Lifetime
Also Published As
Publication number | Publication date |
---|---|
US7547535B2 (en) | 2009-06-16 |
EP1332216A1 (en) | 2003-08-06 |
PL362548A1 (en) | 2004-11-02 |
JP3845618B2 (en) | 2006-11-15 |
US7132270B2 (en) | 2006-11-07 |
US20060148056A1 (en) | 2006-07-06 |
BR0114962A (en) | 2003-10-28 |
WO2002034919A1 (en) | 2002-05-02 |
ATE520777T1 (en) | 2011-09-15 |
JP2004512047A (en) | 2004-04-22 |
BRPI0114962B1 (en) | 2016-07-12 |
JP3889434B2 (en) | 2007-03-07 |
EP1332216B1 (en) | 2011-08-17 |
PL205561B1 (en) | 2010-05-31 |
JP2006314322A (en) | 2006-11-24 |
CA2427029C (en) | 2010-02-02 |
BRPI0114962B8 (en) | 2021-07-27 |
CN1288246C (en) | 2006-12-06 |
AU1596602A (en) | 2002-05-06 |
CN1578836A (en) | 2005-02-09 |
HK1074217A1 (en) | 2005-11-04 |
US20030104595A1 (en) | 2003-06-05 |
KR20030048447A (en) | 2003-06-19 |
US20040005683A1 (en) | 2004-01-08 |
KR100519902B1 (en) | 2005-10-10 |
AU2002215966B2 (en) | 2006-05-04 |
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Legal Events
Date | Code | Title | Description |
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EEER | Examination request | ||
MKEX | Expiry |
Effective date: 20211020 |