Sandbox Reserved 772: Difference between revisions
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==Histidinol Dehydrogenase== | ==Histidinol Dehydrogenase== | ||
Histidinol dehydrogenase (HDH) is coded by the structural gene hisD. Histidinol dehydrogenase catalyzes the last step in the histidine biosynthetic pathway. This pathway was found in bacteria, archaebacteria, fungi, and plants. The pathway involves the conversion of L-histidinol to L-histidine with a L-histidinaldehyde intermediate <ref name=" | Histidinol dehydrogenase (HDH) is coded by the structural gene hisD. Histidinol dehydrogenase catalyzes the last step in the histidine biosynthetic pathway. This pathway was found in bacteria, archaebacteria, fungi, and plants. The pathway involves the conversion of L-histidinol to L-histidine with a L-histidinaldehyde intermediate <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> | ||
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==General Information== | ==General Information== | ||
'''Gene Name''': hisD <ref name="info"> | '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> | ||
'''Organism''': Escherichia coli (strain K12) <ref name="info"> | '''Organism''': Escherichia coli (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> | ||
'''Classification''': Oxidoreductase | '''Classification''': Oxidoreductase | ||
'''Length''': 434 Amino Acids <ref name="info"> | '''Length''': 434 Amino Acids <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> | ||
'''Chains''': A, B <ref name="cite2"> | '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref> | ||
'''Molecular Weight''': | '''Molecular Weight''': | ||
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==Structure== | ==Structure== | ||
HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), whereas the intertwined dimer possibly results from domain swapping. Two domains display a very similar incomplete Rossmann fold that suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site, residue His-327, participates in acid-base catalysis <ref name=" | HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), whereas the intertwined dimer possibly results from domain swapping. Two domains display a very similar incomplete Rossmann fold that suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site, residue His-327, participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> | ||
48% helical (20 helices; 211 residues) | For the overall structure, it is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues). <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> | ||
16% beta sheet (15 strands; 73 residues) | |||
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[[Image:pathways.jpg]] | [[Image:pathways.jpg]] | ||
This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. <ref name=" | This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> | ||
==References== | ==References== | ||
<references /> | <references /> | ||
Revision as of 04:20, 3 December 2013
| This Sandbox is Reserved from Sep 25, 2013, through Mar 31, 2014 for use in the course "BCH455/555 Proteins and Molecular Mechanisms" taught by Michael B. Goshe at the North Carolina State University. This reservation includes Sandbox Reserved 299, Sandbox Reserved 300 and Sandbox Reserved 760 through Sandbox Reserved 779. |
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Histidinol DehydrogenaseHistidinol Dehydrogenase
Histidinol dehydrogenase (HDH) is coded by the structural gene hisD. Histidinol dehydrogenase catalyzes the last step in the histidine biosynthetic pathway. This pathway was found in bacteria, archaebacteria, fungi, and plants. The pathway involves the conversion of L-histidinol to L-histidine with a L-histidinaldehyde intermediate [1]
General InformationGeneral Information
Gene Name: hisD [2]
Organism: Escherichia coli (strain K12) [2]
Classification: Oxidoreductase
Length: 434 Amino Acids [2]
Chains: A, B [3]
Molecular Weight:
Isoelectric Point:
Km:
Vmax:
StructureStructure
HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), whereas the intertwined dimer possibly results from domain swapping. Two domains display a very similar incomplete Rossmann fold that suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site, residue His-327, participates in acid-base catalysis [1]
For the overall structure, it is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues). [4]
Related Structures: 1KAE and 1KAR
Enzymatic MechanismEnzymatic Mechanism
This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. [1]