4-Hydroxy-tetrahydrodipicolinate reductase from Neisseria gonorrhoeae - structure and interactions with coenzymes and substrate analog
Copyright © 2018 Elsevier Inc. All rights reserved..
Neisseria gonorrhoeae, an obligate human pathogen, is a leading cause of communicable diseases globally. Due to rapid development of drug resistance, the rate of successfully curing gonococcal infections is rapidly decreasing. Hence, research is being directed toward finding alternative drugs or drug targets to help eradicate these infections. 4-Hydroxy-tetrahydrodipicolinate reductase (DapB), an important enzyme in the meso-diaminopimelate pathway, is a promising target for the development of new antibiotics. This manuscript describes the first structure of DapB from N. gonorrhoeae determined at 1.85 Å. This enzyme uses NAD(P)H as cofactor. Details of the interactions of the enzyme with its cofactors and a substrate analog/inhibitor are discussed. A large scale bioinformatics analysis of DapBs' sequences is also described.
| Medienart: |
E-Artikel |
|---|
| Erscheinungsjahr: |
2018 |
|---|---|
| Erschienen: |
2018 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:503 |
|---|---|
| Enthalten in: |
Biochemical and biophysical research communications - 503(2018), 3 vom: 10. Sept., Seite 1993-1999 |
| Sprache: |
Englisch |
|---|
| Beteiligte Personen: |
Pote, Swanandi [VerfasserIn] |
|---|
| Links: |
|---|
| Anmerkungen: |
Date Completed 13.05.2019 Date Revised 06.01.2023 published: Print-Electronic Citation Status MEDLINE |
|---|
| doi: |
10.1016/j.bbrc.2018.07.147 |
|---|
| funding: |
|
|---|---|
| Förderinstitution / Projekttitel: |
|
| PPN (Katalog-ID): |
NLM287322394 |
|---|
| LEADER | 01000naa a22002652 4500 | ||
|---|---|---|---|
| 001 | NLM287322394 | ||
| 003 | DE-627 | ||
| 005 | 20231225053743.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 231225s2018 xx |||||o 00| ||eng c | ||
| 024 | 7 | |a 10.1016/j.bbrc.2018.07.147 |2 doi | |
| 028 | 5 | 2 | |a pubmed24n0957.xml |
| 035 | |a (DE-627)NLM287322394 | ||
| 035 | |a (NLM)30093108 | ||
| 035 | |a (PII)S0006-291X(18)31651-6 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 100 | 1 | |a Pote, Swanandi |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a 4-Hydroxy-tetrahydrodipicolinate reductase from Neisseria gonorrhoeae - structure and interactions with coenzymes and substrate analog |
| 264 | 1 | |c 2018 | |
| 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 13.05.2019 | ||
| 500 | |a Date Revised 06.01.2023 | ||
| 500 | |a published: Print-Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Copyright © 2018 Elsevier Inc. All rights reserved. | ||
| 520 | |a Neisseria gonorrhoeae, an obligate human pathogen, is a leading cause of communicable diseases globally. Due to rapid development of drug resistance, the rate of successfully curing gonococcal infections is rapidly decreasing. Hence, research is being directed toward finding alternative drugs or drug targets to help eradicate these infections. 4-Hydroxy-tetrahydrodipicolinate reductase (DapB), an important enzyme in the meso-diaminopimelate pathway, is a promising target for the development of new antibiotics. This manuscript describes the first structure of DapB from N. gonorrhoeae determined at 1.85 Å. This enzyme uses NAD(P)H as cofactor. Details of the interactions of the enzyme with its cofactors and a substrate analog/inhibitor are discussed. A large scale bioinformatics analysis of DapBs' sequences is also described | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, N.I.H., Extramural | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 4 | |a Research Support, U.S. Gov't, Non-P.H.S. | |
| 650 | 4 | |a 2,6-pyridine dicarboxylic acid | |
| 650 | 4 | |a 4-hydroxy-tetrahydrodipicolinate reductase | |
| 650 | 4 | |a Dihydrodipicolinate reductase | |
| 650 | 4 | |a Lysine biosynthesis | |
| 650 | 4 | |a NADH | |
| 650 | 4 | |a NADPH | |
| 650 | 7 | |a Coenzymes |2 NLM | |
| 650 | 7 | |a NADP |2 NLM | |
| 650 | 7 | |a 53-59-8 |2 NLM | |
| 700 | 1 | |a Pye, Sarah E |e verfasserin |4 aut | |
| 700 | 1 | |a Sheahan, Tyler E |e verfasserin |4 aut | |
| 700 | 1 | |a Gawlicka-Chruszcz, Anna |e verfasserin |4 aut | |
| 700 | 1 | |a Majorek, Karolina A |e verfasserin |4 aut | |
| 700 | 1 | |a Chruszcz, Maksymilian |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Biochemical and biophysical research communications |d 1960 |g 503(2018), 3 vom: 10. Sept., Seite 1993-1999 |w (DE-627)NLM000000035 |x 1090-2104 |7 nnns |
| 773 | 1 | 8 | |g volume:503 |g year:2018 |g number:3 |g day:10 |g month:09 |g pages:1993-1999 |
| 856 | 4 | 0 | |u http://dx.doi.org/10.1016/j.bbrc.2018.07.147 |3 Volltext |
| 912 | |a GBV_USEFLAG_A | ||
| 912 | |a GBV_NLM | ||
| 951 | |a AR | ||
| 952 | |d 503 |j 2018 |e 3 |b 10 |c 09 |h 1993-1999 | ||