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
LITERATURE
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
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
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
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
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
-
Histidine metabolism
-
-
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
COMMENTARY
LITERATURE
GcHDH
A1BPP9
-
HDH
-
-
-
-
HIS4 protein
A1BPP9
-
HisD
I6Y6Z1
gene name
HisD
I6Y6Z1
gene name
-
histidinol dehydrogenase
I6Y6Z1
-
histidinol dehydrogenase
I6Y6Z1
-
-
HLDase
-
-
L-histidinol dehydrogenase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9028-27-7
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
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
gene hisD
UniProt
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
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
additional information
-
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
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
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
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
NAD+
-
-
METALS and IONS
ORGANISM
UNIPROT
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
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
HgCl2
-
0.1 mM, 80% inhibition, pH 9.4
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
COMMENTARY
LITERATURE
IMAGE
EDTA
I6Y6Z1
118% activity at 0.1 mM, 135% at 1 mM, slightly inhibitory above 10 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
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]
SUBSTRATE
ORGANISM
UNIPROT
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]
INHIBITOR
ORGANISM
UNIPROT
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
0.000024
(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
-
-
0.000003
(S)-3-amino-1-(4-(benzyloxy)phenyl)-4-(1H-imidazol-4-yl)butan-2-one
-
pH 9.2, 30C
0.000006
(S)-3-amino-1-(4-bromophenyl)-4-(1H-imidazol-4-yl)butan-2-one
-
pH 9.2, 30C
0.000012
(S)-3-amino-1-(4-chlorophenyl)-4-(1H-imidazol-4-yl)butan-2-one
-
pH 9.2, 30C
0.000015
(S)-3-amino-1-(4-fluorophenyl)-4-(1H-imidazol-4-yl)butan-2-one
-
pH 9.2, 30C
0.000016
(S)-3-amino-4-(1H-imidazol-4-yl)-1-(4-phenoxyphenyl)butan-2-one
-
pH 9.2, 30C
0.0000145
(S)-3-amino-4-(1H-imidazol-4-yl)-1-(naphthalen-2-yl)butan-2-one
-
pH 9.2, 30C
0.000015
(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]
ORGANISM
UNIPROT
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
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
ORGANISM
UNIPROT
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8 - 12
-
-
additional information
I6Y6Z1
pH profile, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
I6Y6Z1
assay at
30
-
assay at
37
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
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
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
encoded as proenzyme with amino terminal extension with composition of chloroplast transit peptides
Manually annotated by BRENDA team
-
enzyme contains chloroplast transit peptide sequence
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)
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
91000
-
gel filtration
286332
100000
-
recombinant enzyme expressed in SF9 cells, native PAGE
286327
101800
I6Y6Z1
gel filtration, recombinant enzyme
721426
103000
-
gel filtration
286329
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
P06988
dynamic light scattering
dimer
I6Y6Z1
2 * 45378, sequence calculation, 2 * 45348, recombinant enzyme, mass spectrometry
dimer
-
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
additional information
-
three-dimensional model analysis, overview
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.2 - 10
-
rapid loss of activity above pH 10
286329
TEMPERATURE STABILITY
ORGANISM
UNIPROT
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
286332
70
-
50% activity lost after 2 min
286339
STORAGE STABILITY
ORGANISM
UNIPROT
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
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
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
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
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