1c1d
From Proteopedia
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|PDB= 1c1d |SIZE=350|CAPTION= <scene name='initialview01'>1c1d</scene>, resolution 1.25Å | |PDB= 1c1d |SIZE=350|CAPTION= <scene name='initialview01'>1c1d</scene>, resolution 1.25Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1c1x|1C1X]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c1d OCA], [http://www.ebi.ac.uk/pdbsum/1c1d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1c1d RCSB]</span> | ||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Thoden, J B.]] | [[Category: Thoden, J B.]] | ||
[[Category: Vanhooke, J L.]] | [[Category: Vanhooke, J L.]] | ||
| - | [[Category: IPA]] | ||
| - | [[Category: K]] | ||
| - | [[Category: NA]] | ||
| - | [[Category: NAD]] | ||
| - | [[Category: PHE]] | ||
| - | [[Category: PO4]] | ||
[[Category: amino acid dehydrogenase]] | [[Category: amino acid dehydrogenase]] | ||
[[Category: oxidative deamination mechanism]] | [[Category: oxidative deamination mechanism]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:12:33 2008'' |
Revision as of 16:12, 30 March 2008
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| , resolution 1.25Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , | ||||||
| Related: | 1C1X
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
L-PHENYLALANINE DEHYDROGENASE STRUCTURE IN TERNARY COMPLEX WITH NADH AND L-PHENYLALANINE
Overview
Phenylalanine dehydrogenase catalyzes the reversible, pyridine nucleotide-dependent oxidative deamination of L-phenylalanine to form phenylpyruvate and ammonia. We have characterized the steady-state kinetic behavior of the enzyme from Rhodococcus sp. M4 and determined the X-ray crystal structures of the recombinant enzyme in the complexes, E.NADH.L-phenylalanine and E.NAD(+). L-3-phenyllactate, to 1.25 and 1.4 A resolution, respectively. Initial velocity, product inhibition, and dead-end inhibition studies indicate the kinetic mechanism is ordered, with NAD(+) binding prior to phenylalanine and the products' being released in the order of ammonia, phenylpyruvate, and NADH. The enzyme shows no activity with NADPH or other 2'-phosphorylated pyridine nucleotides but has broad activity with NADH analogues. Our initial structural analyses of the E.NAD(+).phenylpyruvate and E.NAD(+). 3-phenylpropionate complexes established that Lys78 and Asp118 function as the catalytic residues in the active site [Vanhooke et al. (1999) Biochemistry 38, 2326-2339]. We have studied the ionization behavior of these residues in steady-state turnover and use these findings in conjunction with the structural data described both here and in our first report to modify our previously proposed mechanism for the enzymatic reaction. The structural characterizations also illuminate the mechanism of the redox specificity that precludes alpha-amino acid dehydrogenases from functioning as alpha-hydroxy acid dehydrogenases.
About this Structure
1C1D is a Protein complex structure of sequences from Rhodococcus sp.. Full crystallographic information is available from OCA.
Reference
Rhodococcus L-phenylalanine dehydrogenase: kinetics, mechanism, and structural basis for catalytic specificity., Brunhuber NM, Thoden JB, Blanchard JS, Vanhooke JL, Biochemistry. 2000 Aug 8;39(31):9174-87. PMID:10924111
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