Information on EC 1.1.1.23 - histidinol dehydrogenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
1.1.1.23
-
RECOMMENDED NAME
GeneOntology No.
histidinol dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 3 H+
show the reaction diagram
fast reversible oxidation of L-histidanol, followed by slow irreversible hydride transfer from the intermediate L-histidinal
-
L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 3 H+
show the reaction diagram
bi uni uni bi ping pong mechanism, recombinant histidinol dehydrogenase
-
L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 3 H+
show the reaction diagram
also oxidizes L-histidinal
-
L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 3 H+
show the reaction diagram
reaction mechanism, amino acid residues Glu326 and His327 are involved in catalysis
P06988
L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 3 H+
show the reaction diagram
bi uni uni bi ping-pong enzyme mechanism for MtHisD-catalyzed chemical reaction, involves abstraction of the hydroxyl group proton of L-histidinol by His336 and concomitant hydride transfer from the reactive carbon (carbon bound to the hydroxyl group that upon hydride transfer adopts the sp2 configuration) to NAD+, forming L-histidinaldehyde and transiently protonated His336
I6Y6Z1, -
L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 3 H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
Histidine metabolism
-
Metabolic pathways
-
SYSTEMATIC NAME
IUBMB Comments
L-histidinol:NAD+ oxidoreductase
Also oxidizes L-histidinal. The Neurospora enzyme also catalyses the reactions of EC 3.5.4.19 (phosphoribosyl-AMP cyclohydrolase) and EC 3.6.1.31 (phosphoribosyl-ATP diphosphatase).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
HDH
-
-
-
-
HIS4 protein
A1BPP9
-
HisD
I6Y6Z1
gene name
histidinol dehydrogenase
I6Y6Z1
-
HLDase
-
-
L-histidinol dehydrogenase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9028-27-7
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
asparagus shoots
-
-
Manually annotated by BRENDA team
; obtained by transformation
-
-
Manually annotated by BRENDA team
Bacillus subtilis HT1
obtained by transformation
-
-
Manually annotated by BRENDA team
contains probably multiple L-histidinol isoenzymes encoded by different genes
-
-
Manually annotated by BRENDA team
cucumber shoots
-
-
Manually annotated by BRENDA team
lettuce shoots
-
-
Manually annotated by BRENDA team
rose cell culture
-
-
Manually annotated by BRENDA team
eggplant shoots
-
-
Manually annotated by BRENDA team
wheat germ
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
enzyme inhibition leads to inhibition of intracellular bacterial growth in macrophage infection of the facultative intracellular pathogen
metabolism
A1BPP9, -
histidinol dehydrogenase mediates the final step in the histidine biosynthetic pathway
physiological function
-
the enzyme is essential for intramacrophagic replication
metabolism
-
the enzyme catalyzes the last step in histidine biosynthesis
additional information
I6Y6Z1, -
molecular homology model building, overview. His336 plays a critical role in both catalysis and L-Hol binding to MtHisD, Tyr129, Tyr223 and His335 residues make contacts with the substrates in the MtHisD enzyme active site, three-dimensional model analysis, overview
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
-
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
-
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
-
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
-
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
-
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
-
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
-
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
-
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
-
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
ir
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
-
ir
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
-
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
-
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
-
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
-
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
-
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
-
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
-
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
-
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
-
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
ir
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
enzyme is responsible for catalysis of the terminal step in L-histidine biosynthesis, being performed in 2 sequential reactions via the intermediate L-histidinal
-
-
ir
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
Bacillus subtilis HT1
-
-, reaction intermediate
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
show the reaction diagram
-
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
show the reaction diagram
-
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
show the reaction diagram
I6Y6Z1, -
via L-histidinaldehyde intermediate
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
-
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
-
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
-
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
-
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
-
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
-
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
-
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
-
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
-
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
ir
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
P06988
part of L-histidine biosynthesis
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
Bacillus subtilis HT1
-
-
-
?
L-histidinol + NAD+
L-histidinal + NADH + H+
show the reaction diagram
P06988
-
-
-
ir
L-histidinol + NAD+
L-histidinal + NADH + H+
show the reaction diagram
-
-, enzyme is responsible for catalysis of the terminal step in L-histidine biosynthesis, being performed in 2 sequential reactions via the intermediate L-histidinal
-
-
ir
additional information
?
-
A1BPP9, -
ligand-protein interactions in the active site of GcHDH, molecular docking, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
-
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
-
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
-
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
-
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
-
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
-
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
-
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
-
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
-
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
ir
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
reaction intermediate
-
?
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
-
enzyme is responsible for catalysis of the terminal step in L-histidine biosynthesis, being performed in 2 sequential reactions via the intermediate L-histidinal
-
-
ir
L-histidinal + NAD+
L-histidine + NADH
show the reaction diagram
Bacillus subtilis HT1
-
reaction intermediate
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
show the reaction diagram
-
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
show the reaction diagram
I6Y6Z1, -
via L-histidinaldehyde intermediate
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
-
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
-
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
-
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
-
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
-
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
-
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
-
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
-
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
-
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
ir
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
-
-
-
?
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
P06988
part of L-histidine biosynthesis
-
-
?
L-histidinol + NAD+
L-histidinal + NADH + H+
show the reaction diagram
-
enzyme is responsible for catalysis of the terminal step in L-histidine biosynthesis, being performed in 2 sequential reactions via the intermediate L-histidinal
-
-
ir
L-histidinol + NAD+
L-histidine + NADH
show the reaction diagram
Bacillus subtilis HT1
-
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NAD+
P06988
binding site structure
NAD+
I6Y6Z1, -
amino acid residues contributing to NAD+ binding include Tyr129, Gly132, and Asn221 for phosphate binding, Gln193 and Asn221 for adenosine sugar binding, and Phe58, Gln193, and Tyr223 for adenine base binding
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
I6Y6Z1, -
can partially substitute for Zn2+
Cd2+
-
0.02-0.2 mM, 75% increase
Mg2+
I6Y6Z1, -
can partially substitute for Zn2+
Mn2+
-
0.5 mM, 26% increase
Mn2+
-
0.5 mM, 165% increase
Mn2+
I6Y6Z1, -
best activating divalent cation
Zn2+
-
essential for activity, one Zn atom per subunit
Zn2+
-
0.5 mM, 20% increase
Zn2+
P06988
binding site structure
Zn2+
I6Y6Z1, -
required, one Zn2+ bound per subunit of the dimer. Zn2+ ion is octahedrally coordinated to Gln267, His270, Asp369, His428, and two ligands from L-histidinol
Mn2+
-
required
additional information
I6Y6Z1, -
the enzyme is metal-dependent, activity of the apo-enzyme can be rescued by addition of Mn2+, Mg2+, Ca2+, and Zn2+, but not by addition of Cd2+, Co2+ and Ni2+, overview
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(2S)-2-amino-3-(1H-imidazol-4-yl)-N'-(naphthalen-2-ylsulfonyl)propanehydrazide
-
-
(2S)-2-amino-3-(1H-imidazol-4-yl)-N'-[(4-methylphenyl)sulfonyl]propanehydrazide
-
-
(2S)-2-amino-N'-(biphenyl-4-ylsulfonyl)-3-(1H-imidazol-4-yl)propanehydrazide
-
-
(2S)-2-amino-N'-[(4-bromophenyl)sulfonyl]-3-(1H-imidazol-4-yl)propanehydrazide
-
-
(3S)-3-amino-1-(2,3,4,5,6-pentafluorophenyloxy)-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
-
-
(3S)-3-amino-1-(2,3,4,5,6-pentafluorophenylthio)-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
-
-
(3S)-3-amino-1-(4-bromophenoxy)-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
-
-
(3S)-3-amino-1-(4-bromophenylthio)-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
-
-
(3S)-3-amino-1-(4-fluorophenoxy)-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
-
-
(3S)-3-amino-1-(4-fluorophenylthio)-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
-
-
(3S)-3-amino-1-hydroxy-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
-
-
(3S)-3-amino-1-thio-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
-
-
(3S)-3-amino-1-[4-(benzyloxy)phenyl]-4-(1H-imidazol-4-yl)butan-2-one
-
-
(3S)-3-amino-1-[4-(biphenyl-4-ylethynyl)phenyl]-4-(1H-imidazol-4-yl)butan-2-one
-
-
(3S)-3-amino-1-[4-(biphenyl-4-ylmethoxy)phenyl]-4-(1H-imidazol-4-yl)butan-2-one
-
-
(3S)-3-amino-1-[4-[(4-bromobenzyl)oxy]phenyl]-4-(1H-imidazol-4-yl)butan-2-one
-
-
(3S)-3-amino-1-[4-[(4-butylbenzyl)oxy]phenyl]-4-(1H-imidazol-4-yl)butan-2-one
-
50% inhibition of pathogen growth in minimal medium at 0.5 mM
(3S)-3-amino-1-[4-[(4-tert-butylphenyl)ethynyl]phenyl]-4-(1H-imidazol-4-yl)butan-2-one
-
30% inhibition of pathogen growth in minimal medium at 0.5 mM
(3S)-3-amino-1-[4-[(E)-2-(biphenyl-4-yl)ethenyl]phenyl]-4-(1H-imidazol-4-yl)butan-2-one
-
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(4-[(E)-2-[4-(trifluoromethyl)phenyl]ethenyl]phenyl)butan-2-one
-
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(4-[[4-(naphthalen-2-yl)benzyl]oxy]phenyl)butan-2-one
-
complete inhibition of pathogen growth in minimal medium at 0.5 mM
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(4-[[4-(trifluoromethyl)benzyl]oxy]phenyl)butan-2-one
-
70% inhibition of pathogen growth in minimal medium at 0.5 mM
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(naphthalen-2-yloxy)butan-2-one dihydrochloride
-
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(naphthalen-2-ylthio)butan-2-one dihydrochloride
-
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(p-tolyloxy)butan-2-one dihydrochloride
-
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(phenyloxy)butan-2-one dihydrochloride
-
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(phenylthio)butan-2-one dihydrochloride
-
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(tolylthio)butan-2-one dihydrochloride
-
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-(2-phenylethyl)phenyl]butan-2-one
-
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-(phenylethynyl)phenyl]butan-2-one
-
complete inhibition of pathogen growth in minimal medium at 0.5 mM
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(1E)-3-phenylprop-1-en-1-yl]phenyl]butan-2-one
-
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(4-methoxybenzyl)oxy]phenyl]butan-2-one
-
30% inhibition of pathogen growth in minimal medium at 0.5 mM
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(4-methylbenzyl)oxy]phenyl]butan-2-one
-
30% inhibition of pathogen growth in minimal medium at 0.5 mM
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(4-methylphenyl)ethynyl]phenyl]butan-2-one
-
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(4-pentylphenyl)ethynyl]phenyl]butan-2-one
-
30% inhibition of pathogen growth in minimal medium at 0.5 mM
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(4-phenoxybenzyl)oxy]phenyl]butan-2-one
-
70% inhibition of pathogen growth in minimal medium at 0.5 mM
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(E)-2-(4-methylphenyl)ethenyl]phenyl]butan-2-one
-
complete inhibition of pathogen growth in minimal medium at 0.5 mM
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(E)-2-phenylethenyl]phenyl]butan-2-one
-
-
(7R)-1,3-diiodo-5-oxo-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidine-7-carboxylic acid
-
weaker inhibitor
(S)-3-amino-1-(4-(benzyloxy)phenyl)-4-(1H-imidazol-4-yl)butan-2-one
-
-
(S)-3-amino-1-(4-bromophenyl)-4-(1H-imidazol-4-yl)butan-2-one
-
growth of cells is inhibited in minimal medium, multiplication of cells in human macrophages is totally abolished. No biological effect in rich medium
(S)-3-amino-1-(4-bromophenyl)-4-(1H-imidazol-4-yl)butan-2-one
-
-
(S)-3-amino-1-(4-chlorophenyl)-4-(1H-imidazol-4-yl)butan-2-one
-
growth of cells is inhibited in minimal medium, multiplication of cells in human macrophages is totally abolished. No biological effect in rich medium
(S)-3-amino-1-(4-chlorophenyl)-4-(1H-imidazol-4-yl)butan-2-one
-
-
(S)-3-amino-1-(4-fluorophenyl)-4-(1H-imidazol-4-yl)butan-2-one
-
-
(S)-3-amino-4-(1H-imidazol-4-yl)-1-(4-phenoxyphenyl)butan-2-one
-
-
(S)-3-amino-4-(1H-imidazol-4-yl)-1-(naphthalen-2-yl)butan-2-one
-
growth of cells is inhibited in minimal medium, multiplication of cells in human macrophages is totally abolished. No biological effect in rich medium
(S)-3-amino-4-(1H-imidazol-4-yl)-1-(naphthalen-2-yl)butan-2-one
-
-
(S)-3-amino-4-(1H-imidazol-4-yl)-1-p-tolylbutan-2-one
-
-
1,10-phenanthroline
I6Y6Z1, -
54% inhibition at 1 mM, 96% at 5 mM
1,3-diiodo-5-oxo-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidine-7-carboxylic acid
A1BPP9, -
-
3-(1H-imidazol-4-yl)propanoic acid
A1BPP9, -
-
5-oxo-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidine-7-carboxylic acid
A1BPP9, -
i.e. RJ-278
7,8-dihydroimidazo[1,5-c]pyrimidin-5(6H)-one
-
most active inhibitor
7,8-dihydroimidazo[1,5-c]pyrimidin-5(6H)-one
A1BPP9, -
-
7-chloro-4-nitro-2,1,3-benzoxadiazole
-
0.1 mM, pseudo first order inactivation, binds to Cys-116 in active site
Ba2+
-
0.5 mM, 35% inhibition
Borate
-
10 mM, 90% inhibition
Ca2+
-
0.5 mM, 64% inhibition
Cu2+
-
0.5 mM, 76% inhibition
EDTA
-
30 mM, 50% inhibition at pH 7.5
EDTA
I6Y6Z1, -
118% activity at 0.1 mM, 135% at 1 mM, slightly inhibitory above 10 mM
HgCl2
-
0.5 mM, 100% inhibition, 0.05 mM 79% inhibition
imidazole-4-carboxylic acid
-
most active inhibitor
methyl (7R)-1-chloro-5-oxo-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidine-7-carboxylate
-
weaker inhibitor
methyl 1-chloro-5-oxo-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidine-7-carboxylate
A1BPP9, -
-
methyl 1-methyl-N-(phenoxycarbonyl)histidinate
A1BPP9, -
-
methyl 3-(1H-imidazol-4-yl)propanoate
-
-
methyl N-(ethoxycarbonyl)-1-methyl-L-histidinate
-
-
methyl N-(methoxycarbonyl)-3-methyl-L-histidinate
-
-
methyl N-(methoxycarbonyl)histidinate
A1BPP9, -
-
N-(4-dimethylamino-3,5-dinitrophenyl)-maleimide
-
75% inhibition with one equivalent per subunit
N-(4-dimethylamino-3,5-dinitrophenyl)-maleimide
-
-
Ni2+
-
0.5 mM, 54% inhibition
p-chloromercuribenzoate
-
75% inhibition with two equivalents per subunit
p-chloromercuribenzoate
-
2.5 mM, 60% inhibition
p-chloromercuribenzoate
-
0.02 mM, 50% inhibition
pyridoxal 5'-phosphate
-
100 mM, 62.5% inhibition, concentration dependent, almost completely reversible
Urea
-
2.2 mM, 50% inhibition, reversible
Zn2+
-
0.5 mM, 66% inhibition
Mg2+
-
0.5 mM, 46% inhibition
additional information
-
5% dimethyl sulfoxide or methyl N-[(trifluoromethoxy)carbonyl]-L-histidinate trifluoroacetate fails to exert any growth inhibitory activity
-
additional information
A1BPP9, -
screening of substrate analog inhibitors of histidinol dehydrogenase, and docking analysis of these antifungal agents, overview
-
additional information
-
synthesis and evaluation of alpha-O-arylketones and alpha-S-arylketones derived from histidine
-
additional information
-
design, synthesis and evaluation of 19 potential HDH inhibitors, molecular modeling and docking study, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
EDTA
I6Y6Z1, -
118% activity at 0.1 mM, 135% at 1 mM, slightly inhibitory above 10 mM
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0027
-
L-Histidinol
-
-
0.0049
-
L-Histidinol
I6Y6Z1, -
recombinant enzyme, pH 7.2, 25C
0.009
-
L-Histidinol
-
-
0.01
-
L-Histidinol
-
recombinant enzyme
0.012
-
L-Histidinol
-
-
0.016
-
L-Histidinol
-
-
0.05
-
NAD+
-
recombinant enzyme
0.051
-
NAD+
-
-
0.053
-
NAD+
-
-
0.57
-
NAD+
-
-
1.4
-
NAD+
I6Y6Z1, -
recombinant enzyme, pH 7.2, 25C
additional information
-
additional information
I6Y6Z1, -
steady-state kinetics
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.1
-
L-Histidinol
-
-
1.45
-
L-Histidinol
I6Y6Z1, -
recombinant enzyme, pH 7.2, 25C
35
-
L-Histidinol
-
recombinant enzyme without transit peptide
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.14
-
(2S)-2-amino-3-(1H-imidazol-4-yl)-N'-(naphthalen-2-ylsulfonyl)propanehydrazide
-
pH 9.2, 30C
0.16
-
(2S)-2-amino-3-(1H-imidazol-4-yl)-N'-[(4-methylphenyl)sulfonyl]propanehydrazide
-
pH 9.2, 30C
0.025
-
(2S)-2-amino-N'-(biphenyl-4-ylsulfonyl)-3-(1H-imidazol-4-yl)propanehydrazide
-
pH 9.2, 30C
0.07
-
(2S)-2-amino-N'-[(4-bromophenyl)sulfonyl]-3-(1H-imidazol-4-yl)propanehydrazide
-
pH 9.2, 30C
0.0028
-
(3S)-3-amino-1-(2,3,4,5,6-pentafluorophenyloxy)-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
-
pH 9.2, 30C, recombinant His6-tagged enzyme
0.0192
-
(3S)-3-amino-1-(2,3,4,5,6-pentafluorophenylthio)-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
-
pH 9.2, 30C, recombinant His6-tagged enzyme
0.0016
-
(3S)-3-amino-1-(4-bromophenoxy)-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
-
pH 9.2, 30C, recombinant His6-tagged enzyme
0.0028
-
(3S)-3-amino-1-(4-bromophenylthio)-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
-
pH 9.2, 30C, recombinant His6-tagged enzyme
0.0047
-
(3S)-3-amino-1-(4-fluorophenoxy)-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
-
pH 9.2, 30C, recombinant His6-tagged enzyme
0.0031
-
(3S)-3-amino-1-(4-fluorophenylthio)-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
-
pH 9.2, 30C, recombinant His6-tagged enzyme
2.4e-05
-
(3S)-3-amino-1-hydroxy-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
-
pH 9.2, 30C, recombinant His6-tagged enzyme
0.0021
-
(3S)-3-amino-1-thio-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
-
pH 9.2, 30C, recombinant His6-tagged enzyme
3
-
(3S)-3-amino-1-[4-(benzyloxy)phenyl]-4-(1H-imidazol-4-yl)butan-2-one
-
pH and temperature not specified in the publication
40
-
(3S)-3-amino-1-[4-[(4-butylbenzyl)oxy]phenyl]-4-(1H-imidazol-4-yl)butan-2-one
-
pH and temperature not specified in the publication
65
-
(3S)-3-amino-1-[4-[(4-tert-butylphenyl)ethynyl]phenyl]-4-(1H-imidazol-4-yl)butan-2-one
-
pH and temperature not specified in the publication
65
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(4-[(E)-2-[4-(trifluoromethyl)phenyl]ethenyl]phenyl)butan-2-one
-
pH and temperature not specified in the publication
30
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(4-[[4-(naphthalen-2-yl)benzyl]oxy]phenyl)butan-2-one
-
pH and temperature not specified in the publication
30
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(4-[[4-(trifluoromethyl)benzyl]oxy]phenyl)butan-2-one
-
pH and temperature not specified in the publication
0.00011
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(naphthalen-2-yloxy)butan-2-one dihydrochloride
-
pH 9.2, 30C, recombinant His6-tagged enzyme
0.0033
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(naphthalen-2-ylthio)butan-2-one dihydrochloride
-
pH 9.2, 30C, recombinant His6-tagged enzyme
0.00021
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(p-tolyloxy)butan-2-one dihydrochloride
-
pH 9.2, 30C, recombinant His6-tagged enzyme
0.0037
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(phenyloxy)butan-2-one dihydrochloride
-
pH 9.2, 30C, recombinant His6-tagged enzyme
0.0071
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(phenylthio)butan-2-one dihydrochloride
-
pH 9.2, 30C, recombinant His6-tagged enzyme
0.0395
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(tolylthio)butan-2-one dihydrochloride
-
pH 9.2, 30C, recombinant His6-tagged enzyme
13
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-(2-phenylethyl)phenyl]butan-2-one
-
pH and temperature not specified in the publication
3
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-(phenylethynyl)phenyl]butan-2-one
-
pH and temperature not specified in the publication
30
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(1E)-3-phenylprop-1-en-1-yl]phenyl]butan-2-one
-
pH and temperature not specified in the publication
20
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(4-methoxybenzyl)oxy]phenyl]butan-2-one
-
pH and temperature not specified in the publication
30
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(4-methylbenzyl)oxy]phenyl]butan-2-one
-
pH and temperature not specified in the publication
40
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(4-methylphenyl)ethynyl]phenyl]butan-2-one
-
pH and temperature not specified in the publication
8.5
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(4-pentylphenyl)ethynyl]phenyl]butan-2-one
-
pH and temperature not specified in the publication
70
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(4-phenoxybenzyl)oxy]phenyl]butan-2-one
-
pH and temperature not specified in the publication
40
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(E)-2-(4-methylphenyl)ethenyl]phenyl]butan-2-one
-
pH and temperature not specified in the publication
25
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(E)-2-phenylethenyl]phenyl]butan-2-one
-
pH and temperature not specified in the publication
0.0587
-
(7R)-1,3-diiodo-5-oxo-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidine-7-carboxylic acid
-
-
3e-06
-
(S)-3-amino-1-(4-(benzyloxy)phenyl)-4-(1H-imidazol-4-yl)butan-2-one
-
pH 9.2, 30C
6e-06
-
(S)-3-amino-1-(4-bromophenyl)-4-(1H-imidazol-4-yl)butan-2-one
-
pH 9.2, 30C
1.2e-05
-
(S)-3-amino-1-(4-chlorophenyl)-4-(1H-imidazol-4-yl)butan-2-one
-
pH 9.2, 30C
1.5e-05
-
(S)-3-amino-1-(4-fluorophenyl)-4-(1H-imidazol-4-yl)butan-2-one
-
pH 9.2, 30C
1.6e-05
-
(S)-3-amino-4-(1H-imidazol-4-yl)-1-(4-phenoxyphenyl)butan-2-one
-
pH 9.2, 30C
1.45e-05
-
(S)-3-amino-4-(1H-imidazol-4-yl)-1-(naphthalen-2-yl)butan-2-one
-
pH 9.2, 30C
1.5e-05
-
(S)-3-amino-4-(1H-imidazol-4-yl)-1-p-tolylbutan-2-one
-
pH 9.2, 30C
0.0587
-
1,3-diiodo-5-oxo-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidine-7-carboxylic acid
A1BPP9, -
pH not specified in the publication, temperature not specified in the publication
0.00317
-
3-(1H-imidazol-4-yl)propanoic acid
A1BPP9, -
pH not specified in the publication, temperature not specified in the publication
0.00356
-
5-oxo-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidine-7-carboxylic acid
A1BPP9, -
pH not specified in the publication, temperature not specified in the publication
0.0242
-
7,8-dihydroimidazo[1,5-c]pyrimidin-5(6H)-one
-
-
0.0242
-
7,8-dihydroimidazo[1,5-c]pyrimidin-5(6H)-one
A1BPP9, -
pH not specified in the publication, temperature not specified in the publication
0.0064
-
imidazole-4-carboxylic acid
-
-
0.1222
-
methyl (7R)-1-chloro-5-oxo-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidine-7-carboxylate
-
-
0.1222
-
methyl 1-chloro-5-oxo-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidine-7-carboxylate
A1BPP9, -
pH not specified in the publication, temperature not specified in the publication
0.0293
-
methyl 1-methyl-N-(phenoxycarbonyl)histidinate
A1BPP9, -
pH not specified in the publication, temperature not specified in the publication
0.0052
-
methyl 3-(1H-imidazol-4-yl)propanoate
-
-
0.0052
-
methyl 3-(1H-imidazol-4-yl)propanoate
A1BPP9, -
pH not specified in the publication, temperature not specified in the publication
0.0293
-
methyl N-(ethoxycarbonyl)-1-methyl-L-histidinate
-
-
0.0106
-
methyl N-(methoxycarbonyl)-3-methyl-L-histidinate
-
-
0.0106
-
methyl N-(methoxycarbonyl)histidinate
A1BPP9, -
pH not specified in the publication, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0003
-
-
enriched extracts
0.0004
-
-
enriched extracts
0.0009
-
-
enriched extracts
0.0016
-
-
enriched extracts
0.0021
-
-
enriched extracts
0.0061
-
-
enriched extracts
0.0062
-
-
enriched extracts
1.2
-
I6Y6Z1, -
purified recombinant enzyme, pH 7.2, 25C
10
-
-
recombinant enzym
12.71
-
-
-
15.32
-
-
-
additional information
-
-
the activity of the enzyme in different tissues at different pH values, development of a determination method for quantification of L-histidinol and L-histidine using isocratic HPLC, overview
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.2
-
I6Y6Z1, -
assay at
8.6
-
-
crude extracts
8.7
-
-
partly purified enzyme
9.2
-
-
recombinant enzyme
9.2
-
-
purified from cabbage heads
9.2
-
-
assay at
additional information
-
-
the activity of the enzyme in different tissues is differently regulated with respect to the pH value, overview
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8
12
-
-
additional information
-
I6Y6Z1, -
pH profile, overview
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
I6Y6Z1, -
assay at
30
-
-
assay at
37
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
very low activity
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
-
highest activity
Manually annotated by BRENDA team
additional information
-
activity in the organs in descending order: liver, kidney, pancreas, spleen, skeletal muscle, small intestine
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
enzyme contains chloroplast transit peptide sequence
Manually annotated by BRENDA team
-
encoded as proenzyme with amino terminal extension with composition of chloroplast transit peptides
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Brucella suis biovar 1 (strain 1330)
Brucella suis biovar 1 (strain 1330)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
91000
-
-
gel filtration
100000
-
-
recombinant enzyme expressed in SF9 cells, native PAGE
101800
-
I6Y6Z1, -
gel filtration, recombinant enzyme
103000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
P06988
dynamic light scattering
dimer
I6Y6Z1, -
2 * 45378, sequence calculation, 2 * 45348, recombinant enzyme, mass spectrometry
homodimer
-
alpha,alpha, 2 * 52000, SDS-PAGE
homodimer
-
alpha,alpha, 2 * 52000, SDS-PAGE
homodimer
-
alpha,alpha, 2 * 43000, SDS-PAGE
homodimer
A1BPP9, -
structure modelling, overview
additional information
A1BPP9, -
Geotrichum candidum HIS4 protein has HIS4A, HIS4B, and HIS4C subregions
additional information
I6Y6Z1, -
three-dimensional model analysis, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
15.4 mg/ml purified recombinant detagged enzyme alone or complexed with L-histidinol, L-histamine, or L-histidine or Zn2+ and NAD+, in 20 mM Tris-HCl, pH 7.5, 0.2 M NaCl, 5 mM DTT, 1 mM ligand, hanging drop vapour diffusion method, 18C, 0.002 ml protein solution with 0.004 ml reservoir solution, containing 20% w/v PEG 3350, 7% v/v glycerol, 0.1 M imidazole-malic acid, pH 5.5, 0.2 M ammonium sulfate, 2 weeks, macroseeding for larger crystals, transfer to sodium acetate, pH 5.5, to eliminate the inhibiting imidazole, X-ray diffraction structure determination and analysis at 2.2 A resolution, modelling
P06988
1.6-2.0 mM ammonium sulfate solution at 4C, pH 6.5, space group C2, monoclinic
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
9.2
10
-
rapid loss of activity above pH 10
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
65
-
-
almost no loss of activity after 5 min at pH 7.5, histidinol, 2 mM and MnCl2, 1 mM, protect enzyme from heat inactivation
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, 1 week, 10%
-
4C, 20% glycerol, 1 week, 0%
-
0C, 0.05 M Tris-maleate, pH 6.5, 0.1 mM MnCl2, 3 months, 45%
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ammonium sulfate precipitation, DEAE-chromatography, L-histidinol-Sepharose 4B affinity chromatography
-
enzyme expressed in SF9 cells, cell homogenate, Mono Q FPLC
-
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by cobalt affinity chromatography
-
recombinant protein
-
55C, 40% ammonium sulfate, Sephadex G-50, DEAE-cellulose, crystallization
-
60C, pH 5 treatment, ammonium sulfate precipitation, gel filtration, DEAE-cellulose, gel filtration
-
recombinant enzyme fusion protein
P06988
ammonium sulfate precipitation, heating, affinity chromatography, preparative gel
-
recombinant enzyme from Escherichia coli strain BL21(DE3) 40fold to homogeneity by anion exchange chromatography, ultrafiltration, gel filtration, and another step of anion exchange chromatography
I6Y6Z1, -
55C, 40% ammonium sulfate, Sephadex G-50, DEAE-cellulose, crystallization
-
heating, pH 4.8, ammonium sulfate, DEAE-cellulose
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Spodoptera frugiperda, SF9 cells
-
recombinant expression of the His6-tagged enzyme in Escherichia coli strain BL21(DE3)
-
expression in Escherichia coli
-
gene hisD, expression as glutathione S-transferase fusion protein with a thrombin cleavage site between tag and enzyme
P06988
gene hisD, overexpression in Escherichia coli strain BL21(DE3)
I6Y6Z1, -
expressed in Spodoptera frugiperda, SF9 cells
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C112A
-
conserved Cys-112 is not involved in catalysis, Cys-112 corresponds to Cys-116 in Salmonella typhimurium
H261N
-
mutation causes complete loss of Zn and activity
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
drug development
-
histidinol dehydrogenase is a suitable target for not only for Geotrichum candidum but also for related species, wherby compounds identified can serve as a valuable lead for development of novel non-classical antifungal therapy, notably against strain like Candida rapidly becoming resistant to conventional therapy