2bkv
From Proteopedia
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- | [[Image:2bkv.gif|left|200px]] | + | [[Image:2bkv.gif|left|200px]] |
- | + | ||
- | '''STRUCTURE AND KINETICS OF A MONOMERIC GLUCOSAMINE-6-PHOSPHATE DEAMINASE: MISSING LINK OF THE NAGB SUPERFAMILY''' | + | {{Structure |
+ | |PDB= 2bkv |SIZE=350|CAPTION= <scene name='initialview01'>2bkv</scene>, resolution 1.504Å | ||
+ | |SITE= <scene name='pdbsite=AC1:Pga+Binding+Site+For+Chain+B'>AC1</scene> | ||
+ | |LIGAND= <scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC ACID'>PGA</scene> | ||
+ | |ACTIVITY= [http://en.wikipedia.org/wiki/Glucosamine-6-phosphate_deaminase Glucosamine-6-phosphate deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.99.6 3.5.99.6] | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''STRUCTURE AND KINETICS OF A MONOMERIC GLUCOSAMINE-6-PHOSPHATE DEAMINASE: MISSING LINK OF THE NAGB SUPERFAMILY''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2BKV is a [ | + | 2BKV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BKV OCA]. |
==Reference== | ==Reference== | ||
- | Structure and kinetics of a monomeric glucosamine 6-phosphate deaminase: missing link of the NagB superfamily?, Vincent F, Davies GJ, Brannigan JA, J Biol Chem. 2005 May 20;280(20):19649-55. Epub 2005 Mar 8. PMID:[http:// | + | Structure and kinetics of a monomeric glucosamine 6-phosphate deaminase: missing link of the NagB superfamily?, Vincent F, Davies GJ, Brannigan JA, J Biol Chem. 2005 May 20;280(20):19649-55. Epub 2005 Mar 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15755726 15755726] |
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Glucosamine-6-phosphate deaminase]] | [[Category: Glucosamine-6-phosphate deaminase]] | ||
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[[Category: substrate inhibition]] | [[Category: substrate inhibition]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:03:15 2008'' |
Revision as of 14:03, 20 March 2008
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, resolution 1.504Å | |||||||
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Activity: | Glucosamine-6-phosphate deaminase, with EC number 3.5.99.6 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
STRUCTURE AND KINETICS OF A MONOMERIC GLUCOSAMINE-6-PHOSPHATE DEAMINASE: MISSING LINK OF THE NAGB SUPERFAMILY
Overview
Glucosamine 6-phosphate is converted to fructose 6-phosphate and ammonia by the action of the enzyme glucosamine 6-phosphate deaminase, NagB. This reaction is the final step in the specific GlcNAc utilization pathway and thus decides the metabolic fate of GlcNAc. Sequence analyses suggest that the NagB "superfamily" consists of three main clusters: multimeric and allosterically regulated glucosamine-6-phosphate deaminases (exemplified by Escherichia coli NagB), phosphogluconolactonases, and monomeric hexosamine-6-phosphate deaminases. Here we present the three-dimensional structure and kinetics of the first member of this latter group, the glucosamine-6-phosphate deaminase, NagB, from Bacillus subtilis. The structures were determined in ligand-complexed forms at resolutions around 1.4 Angstroms. BsuNagB is monomeric in solution and as a consequence is active (k(cat) 28 s(-1), K(m(app)) 0.13 mM) without the need for allosteric activators. A decrease in activity at high substrate concentrations may reflect substrate inhibition (with K(i) of approximately 4 mM). The structure completes the NagB superfamily structural landscape and thus allows further interrogation of genomic data in terms of the regulation of NagB and the metabolic fate(s) of glucosamine 6-phosphate.
About this Structure
2BKV is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Structure and kinetics of a monomeric glucosamine 6-phosphate deaminase: missing link of the NagB superfamily?, Vincent F, Davies GJ, Brannigan JA, J Biol Chem. 2005 May 20;280(20):19649-55. Epub 2005 Mar 8. PMID:15755726
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