|
|
|
|
LEADER |
03153cam a2200577 4500 |
001 |
0-1024081079 |
003 |
DE-627 |
005 |
20220708170131.0 |
007 |
cr uuu---uuuuu |
008 |
180607s2017 gw |||||om 00| ||eng c |
015 |
|
|
|a 18,O07
|2 dnb
|
016 |
7 |
|
|a 1160753520
|2 DE-101
|
024 |
7 |
|
|a urn:nbn:de:gbv:7-11858/00-1735-0000-002E-E412-C-1
|2 urn
|
035 |
|
|
|a (DE-627)1024081079
|
035 |
|
|
|a (DE-599)GBV1024081079
|
035 |
|
|
|a (OCoLC)1039543928
|
035 |
|
|
|a (DE-101)1160753520
|
040 |
|
|
|a DE-627
|b ger
|c DE-627
|e rda
|
041 |
|
|
|a eng
|
044 |
|
|
|c XA-DE-NI
|
082 |
0 |
|
|a 570
|q SEPA
|2 22
|
082 |
0 |
4 |
|a 570
|q DE-101
|
100 |
1 |
|
|a Dai, Shao-Bo
|e VerfasserIn
|4 aut
|
245 |
1 |
0 |
|a Mechanistic and structural characterization of thiamine diphosphate dependent enzyme transketolases from human and (E.coli)
|c vorgelegt von Shao-Bo Dai
|
264 |
|
1 |
|a Göttingen
|c 2017
|
300 |
|
|
|a 1 Online-Ressource
|b Illustrationen, Diagramme
|
336 |
|
|
|a Text
|b txt
|2 rdacontent
|
337 |
|
|
|a Computermedien
|b c
|2 rdamedia
|
338 |
|
|
|a Online-Ressource
|b cr
|2 rdacarrier
|
502 |
|
|
|b Dissertation
|c Georg-August-Universität Göttingen
|d 2017
|
520 |
|
|
|a Thiamine diphosphate (ThDP) dependent enzymes are essential in the metabolism of biological systems, and many of these enzymes are extensively used in the biosynthetic of valuable compounds. In this regard, a comprehensive study of the catalytic mechanism of this family of enzymes are demanding, especially high resolution structural information. In this thesis, we present the mechanistic study of transketolase, one representative ThDP dependent enzyme, from several different aspects. First we show that a low barrier hydrogen bond (LBHB) is present in the crystal structure of human transketo...
|
583 |
1 |
|
|a Archivierung/Langzeitarchivierung gewährleistet
|2 pdager
|5 DE-101
|
655 |
|
7 |
|a Hochschulschrift
|0 (DE-588)4113937-9
|0 (DE-627)105825778
|0 (DE-576)209480580
|2 gnd-content
|
700 |
1 |
|
|a Tittmann, Kai
|e AkademischeR BetreuerIn
|4 dgs
|
700 |
1 |
|
|a Ficner, Ralf
|e GutachterIn
|4 oth
|
700 |
1 |
|
|a Ischebeck, Till
|e GutachterIn
|4 oth
|
776 |
0 |
8 |
|i Erscheint auch als
|n Druck-Ausgabe
|a Dai, Shao-Bo
|t Mechanistic and structural characterization of thiamine diphosphate dependent enzyme transketolases from human and (E.coli)
|d Göttingen, 2017
|h 1 Online-Ressource
|w (DE-627)1024081087
|
856 |
4 |
0 |
|u http://hdl.handle.net/11858/00-1735-0000-002E-E412-C
|x Resolving-System
|y Volltext
|z kostenfrei
|3 Volltext
|
856 |
4 |
0 |
|u http://nbn-resolving.org/urn:nbn:de:gbv:7-11858/00-1735-0000-002E-E412-C-1
|x Resolving-System
|y Volltext
|z kostenfrei
|3 Volltext
|
856 |
4 |
0 |
|u http://nbn-resolving.de/urn:nbn:de:gbv:7-11858/00-1735-0000-002E-E412-C-1
|v 2018-07-05
|x Resolving-System
|3 Volltext
|
856 |
4 |
0 |
|u http://d-nb.info/1160753520/34
|v 2018-07-05
|x Langzeitarchivierung Nationalbibliothek
|3 Volltext
|
912 |
|
|
|a GBV-ODiss
|
951 |
|
|
|a BO
|
856 |
4 |
0 |
|u http://nbn-resolving.org/urn:nbn:de:gbv:7-11858/00-1735-0000-002E-E412-C-1
|9 LFER
|
852 |
|
|
|a LFER
|z 2019-05-07T00:00:00Z
|
970 |
|
|
|c OD
|
971 |
|
|
|c EBOOK
|
972 |
|
|
|c EBOOK
|
973 |
|
|
|c EB
|
935 |
|
|
|a lfer
|
980 |
|
|
|a 1024081079
|b 0
|k 1024081079
|c lfer
|
SOLR
_version_ |
1785965233172381696 |
access_facet |
Electronic Resources |
author |
Dai, Shao-Bo |
author2 |
Tittmann, Kai, Ficner, Ralf, Ischebeck, Till |
author2_role |
dgs, oth, oth |
author2_variant |
k t kt, r f rf, r f rf, t i ti, t i ti |
author_facet |
Dai, Shao-Bo, Tittmann, Kai, Ficner, Ralf, Ischebeck, Till |
author_role |
aut |
author_sort |
Dai, Shao-Bo |
author_variant |
s b d sbd |
callnumber-sort |
|
collection |
GBV-ODiss, lfer |
contents |
Thiamine diphosphate (ThDP) dependent enzymes are essential in the metabolism of biological systems, and many of these enzymes are extensively used in the biosynthetic of valuable compounds. In this regard, a comprehensive study of the catalytic mechanism of this family of enzymes are demanding, especially high resolution structural information. In this thesis, we present the mechanistic study of transketolase, one representative ThDP dependent enzyme, from several different aspects. First we show that a low barrier hydrogen bond (LBHB) is present in the crystal structure of human transketo... |
ctrlnum |
(DE-627)1024081079, (DE-599)GBV1024081079, (OCoLC)1039543928, (DE-101)1160753520 |
dewey-full |
570 |
dewey-hundreds |
500 - Science |
dewey-ones |
570 - Life sciences; biology |
dewey-raw |
570 |
dewey-search |
570 |
dewey-sort |
3570 |
dewey-tens |
570 - Life sciences; biology |
facet_912a |
GBV-ODiss |
facet_avail |
Online, Free |
finc_class_facet |
Biologie, Medizin |
fincclass_txtF_mv |
science-biology |
format |
eBook, Thesis |
format_access_txtF_mv |
Thesis |
format_de105 |
Ebook |
format_de14 |
Book, E-Book |
format_de15 |
Book, E-Book |
format_del152 |
Buch |
format_detail_txtF_mv |
text-online-monograph-independent-thesis |
format_dezi4 |
e-Book |
format_finc |
Book, E-Book, Thesis |
format_legacy |
ElectronicBook |
format_legacy_nrw |
Book, E-Book |
format_nrw |
Book, E-Book |
format_strict_txtF_mv |
E-Thesis |
genre |
Hochschulschrift (DE-588)4113937-9 (DE-627)105825778 (DE-576)209480580 gnd-content |
genre_facet |
Hochschulschrift |
geogr_code |
not assigned |
geogr_code_person |
not assigned |
id |
0-1024081079 |
illustrated |
Not Illustrated |
imprint |
Göttingen, 2017 |
imprint_str_mv |
Göttingen, 2017 |
institution |
DE-D117, DE-105, LFER, DE-Ch1, DE-15, DE-14, DE-Zwi2 |
is_hierarchy_id |
|
is_hierarchy_title |
|
kxp_id_str |
1024081079 |
language |
English |
last_indexed |
2023-12-22T07:12:51.866Z |
marc024a_ct_mv |
urn:nbn:de:gbv:7-11858/00-1735-0000-002E-E412-C-1 |
match_str |
dai2017mechanisticandstructuralcharacterizationofthiaminediphosphatedependentenzymetransketolasesfromhumanandecoli |
mega_collection |
Verbunddaten SWB, Lizenzfreie Online-Ressourcen |
misc_de105 |
EBOOK |
oclc_num |
1039543928 |
physical |
1 Online-Ressource; Illustrationen, Diagramme |
publishDate |
2017 |
publishDateSort |
2017 |
publishPlace |
Göttingen |
publisher |
|
record_format |
marcfinc |
record_id |
1024081079 |
recordtype |
marcfinc |
rvk_facet |
No subject assigned |
source_id |
0 |
spelling |
Dai, Shao-Bo VerfasserIn aut, Mechanistic and structural characterization of thiamine diphosphate dependent enzyme transketolases from human and (E.coli) vorgelegt von Shao-Bo Dai, Göttingen 2017, 1 Online-Ressource Illustrationen, Diagramme, Text txt rdacontent, Computermedien c rdamedia, Online-Ressource cr rdacarrier, Dissertation Georg-August-Universität Göttingen 2017, Thiamine diphosphate (ThDP) dependent enzymes are essential in the metabolism of biological systems, and many of these enzymes are extensively used in the biosynthetic of valuable compounds. In this regard, a comprehensive study of the catalytic mechanism of this family of enzymes are demanding, especially high resolution structural information. In this thesis, we present the mechanistic study of transketolase, one representative ThDP dependent enzyme, from several different aspects. First we show that a low barrier hydrogen bond (LBHB) is present in the crystal structure of human transketo..., Archivierung/Langzeitarchivierung gewährleistet pdager DE-101, Hochschulschrift (DE-588)4113937-9 (DE-627)105825778 (DE-576)209480580 gnd-content, Tittmann, Kai AkademischeR BetreuerIn dgs, Ficner, Ralf GutachterIn oth, Ischebeck, Till GutachterIn oth, Erscheint auch als Druck-Ausgabe Dai, Shao-Bo Mechanistic and structural characterization of thiamine diphosphate dependent enzyme transketolases from human and (E.coli) Göttingen, 2017 1 Online-Ressource (DE-627)1024081087, http://hdl.handle.net/11858/00-1735-0000-002E-E412-C Resolving-System Volltext kostenfrei Volltext, http://nbn-resolving.org/urn:nbn:de:gbv:7-11858/00-1735-0000-002E-E412-C-1 Resolving-System Volltext kostenfrei Volltext, http://nbn-resolving.de/urn:nbn:de:gbv:7-11858/00-1735-0000-002E-E412-C-1 2018-07-05 Resolving-System Volltext, http://d-nb.info/1160753520/34 2018-07-05 Langzeitarchivierung Nationalbibliothek Volltext, http://nbn-resolving.org/urn:nbn:de:gbv:7-11858/00-1735-0000-002E-E412-C-1 LFER, LFER 2019-05-07T00:00:00Z |
spellingShingle |
Dai, Shao-Bo, Mechanistic and structural characterization of thiamine diphosphate dependent enzyme transketolases from human and (E.coli), Thiamine diphosphate (ThDP) dependent enzymes are essential in the metabolism of biological systems, and many of these enzymes are extensively used in the biosynthetic of valuable compounds. In this regard, a comprehensive study of the catalytic mechanism of this family of enzymes are demanding, especially high resolution structural information. In this thesis, we present the mechanistic study of transketolase, one representative ThDP dependent enzyme, from several different aspects. First we show that a low barrier hydrogen bond (LBHB) is present in the crystal structure of human transketo..., Hochschulschrift |
title |
Mechanistic and structural characterization of thiamine diphosphate dependent enzyme transketolases from human and (E.coli) |
title_auth |
Mechanistic and structural characterization of thiamine diphosphate dependent enzyme transketolases from human and (E.coli) |
title_full |
Mechanistic and structural characterization of thiamine diphosphate dependent enzyme transketolases from human and (E.coli) vorgelegt von Shao-Bo Dai |
title_fullStr |
Mechanistic and structural characterization of thiamine diphosphate dependent enzyme transketolases from human and (E.coli) vorgelegt von Shao-Bo Dai |
title_full_unstemmed |
Mechanistic and structural characterization of thiamine diphosphate dependent enzyme transketolases from human and (E.coli) vorgelegt von Shao-Bo Dai |
title_short |
Mechanistic and structural characterization of thiamine diphosphate dependent enzyme transketolases from human and (E.coli) |
title_sort |
mechanistic and structural characterization of thiamine diphosphate dependent enzyme transketolases from human and e coli |
title_unstemmed |
Mechanistic and structural characterization of thiamine diphosphate dependent enzyme transketolases from human and (E.coli) |
topic |
Hochschulschrift |
topic_facet |
Hochschulschrift |
url |
http://hdl.handle.net/11858/00-1735-0000-002E-E412-C, http://nbn-resolving.org/urn:nbn:de:gbv:7-11858/00-1735-0000-002E-E412-C-1, http://nbn-resolving.de/urn:nbn:de:gbv:7-11858/00-1735-0000-002E-E412-C-1, http://d-nb.info/1160753520/34 |
urn |
urn:nbn:de:gbv:7-11858/00-1735-0000-002E-E412-C-1 |