1arz
From Proteopedia
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{{STRUCTURE_1arz| PDB=1arz | SCENE= }} | {{STRUCTURE_1arz| PDB=1arz | SCENE= }} | ||
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===ESCHERICHIA COLI DIHYDRODIPICOLINATE REDUCTASE IN COMPLEX WITH NADH AND 2,6 PYRIDINE DICARBOXYLATE=== | ===ESCHERICHIA COLI DIHYDRODIPICOLINATE REDUCTASE IN COMPLEX WITH NADH AND 2,6 PYRIDINE DICARBOXYLATE=== | ||
+ | {{ABSTRACT_PUBMED_9398235}} | ||
- | + | ==Function== | |
+ | [[http://www.uniprot.org/uniprot/DAPB_ECOLI DAPB_ECOLI]] Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. Can use both NADH and NADPH as a reductant, with NADH being twice as effective as NADPH.<ref>PMID:7893644</ref> <ref>PMID:20503968</ref> | ||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID:009398235</ref><references group="xtra"/> | + | <ref group="xtra">PMID:009398235</ref><references group="xtra"/><references/> |
- | [[Category: | + | [[Category: 4-hydroxy-tetrahydrodipicolinate reductase]] |
[[Category: Escherichia coli k-12]] | [[Category: Escherichia coli k-12]] | ||
[[Category: Blanchard, J S.]] | [[Category: Blanchard, J S.]] |
Revision as of 08:34, 30 October 2013
Contents |
ESCHERICHIA COLI DIHYDRODIPICOLINATE REDUCTASE IN COMPLEX WITH NADH AND 2,6 PYRIDINE DICARBOXYLATE
Template:ABSTRACT PUBMED 9398235
Function
[DAPB_ECOLI] Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. Can use both NADH and NADPH as a reductant, with NADH being twice as effective as NADPH.[1] [2]
About this Structure
1arz is a 4 chain structure with sequence from Escherichia coli k-12. Full crystallographic information is available from OCA.
Reference
- Scapin G, Reddy SG, Zheng R, Blanchard JS. Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase in complex with NADH and the inhibitor 2,6-pyridinedicarboxylate. Biochemistry. 1997 Dec 9;36(49):15081-8. PMID:9398235 doi:http://dx.doi.org/10.1021/bi9719915
- ↑ Reddy SG, Sacchettini JC, Blanchard JS. Expression, purification, and characterization of Escherichia coli dihydrodipicolinate reductase. Biochemistry. 1995 Mar 21;34(11):3492-501. PMID:7893644
- ↑ Devenish SR, Blunt JW, Gerrard JA. NMR studies uncover alternate substrates for dihydrodipicolinate synthase and suggest that dihydrodipicolinate reductase is also a dehydratase. J Med Chem. 2010 Jun 24;53(12):4808-12. doi: 10.1021/jm100349s. PMID:20503968 doi:10.1021/jm100349s