Information on EC 4.3.1.3 - histidine ammonia-lyase

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

EC NUMBER
COMMENTARY
4.3.1.3
-
RECOMMENDED NAME
GeneOntology No.
histidine ammonia-lyase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-histidine = urocanate + NH3
show the reaction diagram
-
-
-
-
L-histidine = urocanate + NH3
show the reaction diagram
mechanism
-
L-histidine = urocanate + NH3
show the reaction diagram
mechanism
-
L-histidine = urocanate + NH3
show the reaction diagram
mechanism
-
L-histidine = urocanate + NH3
show the reaction diagram
mechanism
-
L-histidine = urocanate + NH3
show the reaction diagram
mechanism
-
L-histidine = urocanate + NH3
show the reaction diagram
mechanism
Pseudomonas fluorescens A.3.12
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Deamination
-
-
elimination
-
-
elimination
-
-
of NH3, C-N bond cleavage
-
elimination of NH3
-
-
elimination of NH3
-
-
PATHWAY
KEGG Link
MetaCyc Link
histidine degradation I
-
histidine degradation II
-
histidine degradation III
-
histidine degradation VI
-
Histidine metabolism
-
Metabolic pathways
-
SYSTEMATIC NAME
IUBMB Comments
L-histidine ammonia-lyase (urocanate-forming)
This enzyme is a member of the aromatic amino acid lyase family, other members of which are EC 4.3.1.23 (tyrosine ammonia-lyase), EC 4.3.1.24 (phenylalanine ammonia-lyase) and EC 4.3.1.25 (phenylalanine/tyrosine ammonia-lyase). The enzyme contains the cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO), which is common to this family [4]. This unique cofactor is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine [5]. This enzyme catalyses the first step in the degradation of histidine and the product, urocanic acid, is further metabolized to glutamate [2,3].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
ammonia-lyase, histidine
-
-
-
-
HAL
-
-
-
-
histidase
-
-
-
-
histidase, Hut
-
-
-
-
histidinase
-
-
-
-
histidine alpha-deaminase
-
-
-
-
histidine ammonia lyase
-
-
histidine ammonia-lyase
-
-
histidine ammonia-lyase
-
-
histidine deaminase
-
-
-
-
L-HAL
-
-
-
-
L-histidase
-
-
-
-
L-histidine NH3-lyase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9013-75-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Achromobacter liquidum
IAM 1667
-
-
Manually annotated by BRENDA team
Achromobacter liquidum IAM 1667
IAM 1667
-
-
Manually annotated by BRENDA team
Marburg 168
-
-
Manually annotated by BRENDA team
Bacillus subtilis Marburg 168
Marburg 168
-
-
Manually annotated by BRENDA team
Bacillus subtilis W23G
W23G
-
-
Manually annotated by BRENDA team
Chlamydomonas reinhardtii CCAP 11/32A
CCAP 11/32A
-
-
Manually annotated by BRENDA team
sunflower
-
-
Manually annotated by BRENDA team
patients with histidinemia. Identification of four missense mutations within the histidase gene: R322P, P259L, R206T and R208L
-
-
Manually annotated by BRENDA team
Lysinibacillus sphaericus 2362
2362
-
-
Manually annotated by BRENDA team
Salmo gairdnerii Richardson
-
-
Manually annotated by BRENDA team
A.3.12; mutant from ATCC 11250
-
-
Manually annotated by BRENDA team
Pseudomonas fluorescens A.3.12
A.3.12
-
-
Manually annotated by BRENDA team
ATCC 12633
-
-
Manually annotated by BRENDA team
ATCC 12633; PRS1
-
-
Manually annotated by BRENDA team
Pseudomonas putida A.3.12
A.3.12
-
-
Manually annotated by BRENDA team
ATCC 112996; ATCC 11,299b
-
-
Manually annotated by BRENDA team
female Spargue-Dawley
-
-
Manually annotated by BRENDA team
histidase activity is induced in pair-fed rats
-
-
Manually annotated by BRENDA team
Holtzman albion rat
-
-
Manually annotated by BRENDA team
pregnant female Wistar
-
-
Manually annotated by BRENDA team
spinach
-
-
Manually annotated by BRENDA team
ATCC 23921
-
-
Manually annotated by BRENDA team
NRRL B-2682
-
-
Manually annotated by BRENDA team
Streptomyces griseus NRRL B-2682
NRRL B-2682
-
-
Manually annotated by BRENDA team
toad
-
-
-
Manually annotated by BRENDA team
soil samples from the Ap horizont of a black chernozemic soil, Typic Cryoboroll, under grass, dominantly Festuca rubra
-
-
Manually annotated by BRENDA team
Baldi, Giza2; Romi, Equadolze
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-fluorohistidine
2-fluorourocanate + NH3
show the reaction diagram
-
-
-
?
4-fluoro-DL-histidine
4-fluorourocanate + NH3
show the reaction diagram
-
very poor substrate
-
r
4-fluorohistidine
4-fluorourocanate + NH3
show the reaction diagram
-
-
-
-
?
4-nitro-L-histidine
4-nitrourocanate + NH3
show the reaction diagram
-
-
-
-
?
DL-histidine
urocanate + NH3
show the reaction diagram
-
-
-
?
L-aspartate
fumarate + NH3
show the reaction diagram
-
-
-
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
-
-
r
L-histidine
urocanate + NH3
show the reaction diagram
-
-
-
r
L-histidine
urocanate + NH3
show the reaction diagram
-
-
-
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
-
-
r
L-histidine
urocanate + NH3
show the reaction diagram
-
-
-
r
L-histidine
urocanate + NH3
show the reaction diagram
-
-
-
r
L-histidine
urocanate + NH3
show the reaction diagram
-
-
-
r
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
r
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
-
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
-
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
-
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
-
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
-
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
-
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
-
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
r
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
r
L-histidine
urocanate + NH3
show the reaction diagram
P21310
natural substrate
-
r
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
toad
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
Achromobacter liquidum, Helianthus sp.
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
-
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
trans-urocanate
-
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate
enzyme catalyzes amination under extreme condition, 4 M NH4OH, pH 10
r
L-histidine
urocanate + NH3
show the reaction diagram
-
non-oxidative deamination
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
non-oxidative deamination
-
-
L-histidine
urocanate + NH3
show the reaction diagram
-
non-oxidative deamination
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
non-oxidative deamination
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
non-oxidative deamination
-
?
L-histidine
urocanate + NH3
show the reaction diagram
Achromobacter liquidum IAM 1667
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
Bacillus subtilis Marburg 168
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
Lysinibacillus sphaericus 2362
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
Streptomyces griseus NRRL B-2682
-
natural substrate, non-oxidative deamination
-
?
L-histidine
urocanate + NH3
show the reaction diagram
Pseudomonas fluorescens A.3.12
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
Pseudomonas putida A.3.12
-
natural substrate
-
-
L-histidine
urocanate + NH3
show the reaction diagram
Bacillus subtilis W23G
-
natural substrate
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
natural substrate, non-oxidative deamination
-
-
L-histidine
trans-urocanic acid + NH3
show the reaction diagram
-
-
main ultraviolet light absorption factor of the stratum corneum, component of the natural moisturizing factor (mixture of low-molecular weight, watersoluble substances that maintain the proper hydration of the stratum corneum), trans-urocanic acid is implicated in photoaging of human skin
-
?
L-histidine
trans-urocanic acid + NH3
show the reaction diagram
-
enzyme catalyzes the formation of urocanic acid in the skin, modifies risk of basal cell carcinoma and squamous cell carcinoma
urocanic acid is a UV radiation-absorbing molecule in the stratum corneum
-
?
L-histidine methyl ester
urocanate methyl ester
show the reaction diagram
-
cloned enzyme
cloned enzyme
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
?
additional information
?
-
-
catabolite repression of enzyme biosynthesis by acetate
-
-
-
additional information
?
-
-
deficiency of enzyme results in histidinemia
-
-
-
additional information
?
-
-
deficiency of enzyme results in histidinemia
-
-
-
additional information
?
-
-
Ser-143 is an essential active site residue in the enzyme
-
-
-
additional information
?
-
-
histidine utilization is controlled posttranslationally by an activation cascade that involves at least two regulatory proteins
-
-
-
additional information
?
-
-
inductive and repressive effects of carbon and nitrogen on enzyme activity in a black chernozemic soil
-
-
-
additional information
?
-
-
pathway of histidine metabolism, enzymatical synthesis of urocanic acid
-
-
-
additional information
?
-
-
pathway of histidine catabolism
-
-
-
additional information
?
-
-
use of histidine as a nitrogen source is regulated by nitrogen metabolite repression control of histidase synthesis
-
-
-
additional information
?
-
Lysinibacillus sphaericus 2362
-
catabolite repression of enzyme biosynthesis by acetate
-
-
-
additional information
?
-
Pseudomonas fluorescens A.3.12
-
-
-
-
-
additional information
?
-
Pseudomonas putida A.3.12
-
-
-
-
?
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-histidine
urocanate + NH3
show the reaction diagram
-
-
-
r
L-histidine
urocanate + NH3
show the reaction diagram
-
-
-
r
L-histidine
urocanate + NH3
show the reaction diagram
-
-
-
-
?
L-histidine
urocanate + NH3
show the reaction diagram
-
-
-
r
L-histidine
urocanate + NH3
show the reaction diagram
-
-
-
r
L-histidine
urocanate + NH3
show the reaction diagram
-
-
-
r
L-histidine
urocanate + NH3
show the reaction diagram
-
-
-
r
L-histidine
trans-urocanic acid + NH3
show the reaction diagram
-
-
main ultraviolet light absorption factor of the stratum corneum, component of the natural moisturizing factor (mixture of low-molecular weight, watersoluble substances that maintain the proper hydration of the stratum corneum), trans-urocanic acid is implicated in photoaging of human skin
-
?
L-histidine
trans-urocanic acid + NH3
show the reaction diagram
-
enzyme catalyzes the formation of urocanic acid in the skin, modifies risk of basal cell carcinoma and squamous cell carcinoma
urocanic acid is a UV radiation-absorbing molecule in the stratum corneum
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
catabolite repression of enzyme biosynthesis by acetate
-
-
-
additional information
?
-
-
deficiency of enzyme results in histidinemia
-
-
-
additional information
?
-
-
deficiency of enzyme results in histidinemia
-
-
-
additional information
?
-
-
Ser-143 is an essential active site residue in the enzyme
-
-
-
additional information
?
-
-
histidine utilization is controlled posttranslationally by an activation cascade that involves at least two regulatory proteins
-
-
-
additional information
?
-
-
inductive and repressive effects of carbon and nitrogen on enzyme activity in a black chernozemic soil
-
-
-
additional information
?
-
-
pathway of histidine metabolism, enzymatical synthesis of urocanic acid
-
-
-
additional information
?
-
-
pathway of histidine catabolism
-
-
-
additional information
?
-
-
use of histidine as a nitrogen source is regulated by nitrogen metabolite repression control of histidase synthesis
-
-
-
additional information
?
-
Lysinibacillus sphaericus 2362
-
catabolite repression of enzyme biosynthesis by acetate
-
-
-
additional information
?
-
Pseudomonas fluorescens A.3.12
-
-
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
AMP
-
0.016 mM, maximal activity
vitamin B12
-
0.0033 mM, maximal activity
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
activates at a concentration of 0.1 mM
Cd2+
-
stimulates oxidized and reduced enzyme
Cd2+
-
activates at a concentration of 0.1 mM
Fe2+
-
required for optimal activity
Mg2+
-
activates at a concentration of 0.1 mM
Mn2+
-
stimulates oxidized and reduced enzyme
Mn2+
-
enhances activity
Mn2+
-
activates at a concentration of 0.1 mM
Mn2+
-
required
Ni2+
-
activates at a concentration of 0.1 mM
Zn2+
-
required for optimal activity
Zn2+
-
activates at a concentration of 0.1 mM
Mn2+
-
0.1 mM, activation to 124.5% of control
additional information
-
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(2E)-3-(1-benzofuran-2-yl)prop-2-enoic acid
-
-
(2E)-3-(1-benzofuran-3-yl)prop-2-enoic acid
-
-
(2E)-3-(1-benzothiophen-2-yl)prop-2-enoic acid
-
-
(2E)-3-(1-benzothiophen-3-yl)prop-2-enoic acid
-
-
(2E)-3-(1-methyl-1H-indol-3-yl)prop-2-enoic acid
-
-
(2E)-3-(1H-indol-3-yl)prop-2-enoic acid
-
-
(2E)-3-(3-methylfuran-2-yl)prop-2-enoic acid
-
-
(2E)-3-(3-methylthiophen-2-yl)prop-2-enoic acid
-
-
(2E)-3-furan-2-ylprop-2-enoic acid
-
-
(2E)-3-thiophen-2-ylprop-2-enoic acid
-
-
1,2,4-triazole-DL-alanine
Achromobacter liquidum
-
competitive
1-amino-2-imidazol-4'-ylethylphosphonic acid
-
reversible, competitive, 1 mM: complete inhibition
1-Methyltryptophan
-
-
2,3 butanedione
-
-
2-mercaptoethanol
-
inhibition at concentrations above 10 mM, reversed by addition of metal ion
2-methyl-DL-histidine
Achromobacter liquidum
-
competitive
2-thiazolyl-DL-alanine
Achromobacter liquidum
-
competitive
3-(1-benzofuran-2-yl)alanine
-
-
3-(1-benzofuran-3-yl)alanine
-
-
3-(1-benzothiophen-2-yl)alanine
-
-
3-(1-benzothiophen-3-yl)alanine
-
-
3-(3-methylthiophen-2-yl)alanine
-
-
3-furan-2-ylalanine
-
-
3-methyl-L-histidine
Achromobacter liquidum
-
competitive
3-thiophen-2-ylalanine
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
protection of reduced enzyme by Cd2+ against inactivation
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
8-methoxypsoralen
-
noncompetitive. Irradiation of 8-methoxypsoralen with broadband UVA and broadband UVA/UVB results in uncompetitive inhibition due to psoralen-oxidized photoproducts
all-trans retinoic acid
-
1 microM suppresses histidase expression almost completely, levels of histidase mRNA expression in the presence of all-trans retinoic acid are significantly lower on day 2 of post-confluence and at all later time points during keratinocyte differentiation
alpha-methyl-DL-histidine
Achromobacter liquidum
-
competitive
Ba2+
Achromobacter liquidum
-
1 mM
beta-imidazole lactic acid
Achromobacter liquidum
-
competitive
bisulfite
-
sodiumbisulfite
bisulfite
-
10 mM, 95% loss of activity after 90 min, 0.1 mM 1-amino-2-imidazol-4'-ylethylphosphoric acid protects
CN-
-
0.01 M, 40% inhibition
CN-
-
irreversible
Co3+
-
0.1 mM, 95% inhibition
Cu2+
-
0.1 mM, 70% inhibition
cyanide
-
50 mM histidinol phosphate, 5 mM L-histidine and 5 mM Mn2+ protects
D-alpha-hydrazinohistidine
-
competitive
D-alpha-hydrazinoimidazolylpropionic acid
-
strong
D-alpha-hydrazinoimidazolylpropionic acid
-
inactivates in vivo
D-Cysteine
-
in the presence of Cd2+
D-histidine
-
competitive
D-histidine
-
competitive
D-histidine
-
cloned enzyme, reversible competitive
dithiothreitol
-
20 mM, liver and epidermal enzyme, restored by addition with Zn2+
DL-alpha-hydrazinoimidazolylpropionic acid
-
70% irreversible inactivation in vivo
DL-pyrazolyl-3-alanine
-
5.0 mM
EDTA
-
0.001 mM: 50% inhibition, 0.01 mM, complete inhibition
EDTA
-
potent inhibitor of the reduced enzyme; reduced enzyme
EDTA
-
reversed by addition of divalent cations
EDTA
-
0.04 mM, liver and epidermal enzyme, restored by incubation with Zn2+
EDTA
-
0.005 mM, 75% decrease of activity
Fe2+
-
0.1 mM, 60% inhibition
-
Fe3+
Achromobacter liquidum
-
1 mM
-
Fe3+
-
0.1 mM, 60% inhibition
-
formyl-L-histidine
Achromobacter liquidum
-
competitive
glycine
-
0.02 M glycine buffer, 40% inhibition. Inhibition can be overcome by addition of cations, including Mn2+, Ca2+, and Mg2+
H2O2
Achromobacter liquidum
-
-
histidinol phosphate
-
competitive
hydroxylamine
-
-
hydroxymethylimidazole
Achromobacter liquidum
-
competitive
-
imidazol-3-ylpyruvate
-
uncompetitive
-
imidazole
Achromobacter liquidum
-
noncompetitive
interleukin-1alpha
-
treatment of IL-1a reduces histidase expression, the suppressive effect can be reverted by concomitant treatment with interleukin-1alpha receptor antagonist
-
L-1-methylhistidine
-
5.0 mM
L-alanine
-
5.0 mM
L-alpha-hydrazinoimidazolylpropionic acid
-
competitive
-
L-cystein
-
50 mM, complete inaction at basic pH in the presence of O2 is due to a covalent modification of the enzyme
L-cystein
-
10 mM, complete inactivation at pH higher than 10 in the presence of O2
L-cysteine
-
competitive in the presence of EDTA; in the presence of Cd2+; irreversible in the presence of O2
L-cysteine
Achromobacter liquidum
-
-
L-cysteine
-
competitive, cloned enzyme
L-cysteine
-
irreversible
L-cysteine
-
irreversible in the presence of O2
L-cysteine
-
10 mM, irreversible inactivation
L-cysteine
-
10 mM, complete inactivation after 3 h under aerobic conditions
L-histidine hydrazide
Achromobacter liquidum
-
noncompetitive
L-histidine hydroxamate
Achromobacter liquidum, Rattus norvegicus
-
competitive
L-histidine hydroxamate
-
competitive; strong
L-histidine hydroxamate
-
competitive
L-histidinemethyl ester
Achromobacter liquidum, Rattus norvegicus
-
-
L-histidinemethyl ester
-
5.0 mM
L-Histidinol
Achromobacter liquidum
-
competitive
L-Histidinol
-
competitive
L-homocysteine
-
irreversible in the presence of O2 and high pH
L-N-gamma-methylhistidine
-
weak competitive
L-tyrosine
-
heat-purified enzyme, at low concentrations, pH 7-8
N-acetyl-L-histidine
-
5.0 mM
N-ethylmaleimide
-
1 mM, partial
NaBH4
Achromobacter liquidum
-
-
Nitromethane
-
-
Nitromethane
-
inactivates enzyme in vivo
norhistidine
-
-
-
O2
-
irreversible
p-fluoro-L-histidine
-
competitive
-
p-fluoro-L-histidine
-
competitive
-
p-hydroxyphenylpyruvate
-
heat-purified enzyme, at low concentrations, pH 7-8
p-mercuribenzoate
-
inhibits mercaptoethanol-activated enzyme
p-mercuribenzoate
-
0.01 mM, complete inhibition, partially reversed by addition of histidine
p-nitro-L-histidine
-
competitive
-
Pb2+
Achromobacter liquidum
-
1 mM
Phenylglyoxal
-
protection by histidinol phosphate
phenylhydrazine
-
-
Sodium diphosphate
-
-
TGF-alpha
-
most pronounced effect, leads to almost complete suppression of histidase expression
-
TNF-alpha
-
suppresses the expression of histidase
-
Urocanate
-
heat-purified enzyme, at low concentrations, pH 7-8
Methylglyoxal
-
-
additional information
-
-
-
additional information
-
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
activates
2-mercaptoethanol
-
activates at concentrations up to 10 mM
dithiothreitol
-
activates
Estrogen
-
transcriptional activator of histidase expression
glucocorticoid
-
transcriptional activator of histidase expression
-
GSH
-
activates
GSH
-
activates
sulfhydryl compounds
-
activates
sulfhydryl compounds
-
activates
GSH
-
increases at concentrations below 5 mM, pH 7.4
additional information
-
detection of increased trans-urocanic acid levels in the epidermis of patients with psoriasis and in UV-treated epidermis indicates that epidermal histidase may be subject to regulation by endogenous and exogenous factors; expression of histidase strongly increases at the mRNA and protein levels during differentiation of primary keratinocytes in vitro; treatment of keratinocytes with UVA and UVB does not significantly change the expression level of histidase
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
20
-
2-fluorohistidine
-
-
1.25
-
4-fluoro-DL-histidine
-
in the presence of 0.1 mM CdCl2
6.4
-
4-fluoro-DL-histidine
-
in the presence of 1 mM EDTA
5
-
4-fluorourocanate
-
-
2.7
-
DL-histidine
-
in the presence of 0.1 mM CdCl2
10
-
DL-histidine
-
in the presence of 1 mM EDTA
0.2
-
L-histidine
-
pH 9, kidney enzyme
0.36
-
L-histidine
-
pH 9.2 and pH 7.0, epidermal enzyme
0.45
-
L-histidine
-
pH 9.0
0.55
-
L-histidine
-
pH 9.2, liver enzyme
0.6
-
L-histidine
-
-
0.88
-
L-histidine
-
-
1
-
L-histidine
-
pH 7.0, liver enzyme
1.2
-
L-histidine
-
-
1.6
-
L-histidine
-
pH 7
2.1
-
L-histidine
-
pH 7.2
3.6
-
L-histidine
Achromobacter liquidum
-
-
3.8
-
L-histidine
-
25C
3.9
-
L-histidine
-
25C, pH 9.3
5.1
-
L-histidine
-
pH 9
5.3
-
L-histidine
-
native enzyme, pH 9.0
5.8
-
L-histidine
-
cloned enzyme, pH 9.0
6
-
L-histidine
-
oxidized enzyme, in the absence of added metal
6.3
-
L-histidine
-
reduced enzyme in the presence of 0.01 M EDTA
6.7
-
L-histidine
-
-
3
-
Urocanate
-
-
20
-
L-histidine
-
enzyme in solution or microencapsulated
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
the enzyme does not exhibit classical Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
86
-
L-histidine
-
25C, pH 9.3
255
-
L-histidine
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.056
-
(2E)-3-(1-benzofuran-2-yl)prop-2-enoic acid
-
competitive inhibition
0.023
-
(2E)-3-(1-benzofuran-3-yl)prop-2-enoic acid
-
competitive inhibition
0.039
-
(2E)-3-(1-benzothiophen-2-yl)prop-2-enoic acid
-
competitive inhibition
0.053
-
(2E)-3-(1-benzothiophen-3-yl)prop-2-enoic acid
-
competitive inhibition
0.026
-
(2E)-3-(1-methyl-1H-indol-3-yl)prop-2-enoic acid
-
competitive inhibition
0.015
-
(2E)-3-(1H-indol-3-yl)prop-2-enoic acid
-
competitive inhibition
0.018
-
(2E)-3-(3-methylfuran-2-yl)prop-2-enoic acid
-
competitive inhibition
0.04
-
(2E)-3-(3-methylthiophen-2-yl)prop-2-enoic acid
-
competitive inhibition
0.033
-
(2E)-3-furan-2-ylprop-2-enoic acid
-
competitive inhibition
0.041
-
(2E)-3-thiophen-2-ylprop-2-enoic acid
-
competitive inhibition
0.031
-
1-Methyltryptophan
-
mixed inhibition
0.025
-
3-(1-benzofuran-2-yl)alanine
-
competitive inhibition
0.067
-
3-(1-benzofuran-3-yl)alanine
-
competitive inhibition
0.083
-
3-(1-benzothiophen-2-yl)alanine
-
competitive inhibition
0.082
-
3-(1-benzothiophen-3-yl)alanine
-
competitive inhibition
0.098
-
3-(3-methylthiophen-2-yl)alanine
-
competitive inhibition
0.139
-
3-furan-2-ylalanine
-
competitive inhibition
0.101
-
3-thiophen-2-ylalanine
-
competitive inhibition
0.001
-
EDTA
-
-
1.72
-
norhistidine
-
mixed inhibition
-
0.05
-
tryptophan
-
mixed inhibition
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.3427
-
-
native enzyme
1.2
-
-
0.1 mM Ca2+, oxidized enzyme
2.3
-
-
0.1 mM Mn2+, oxidized enzyme
2.8
-
-
0.1 mM Fe2+, oxidized enzyme
3.4
-
-
37C, pH 9.0, 3.3 mM L-histidine
4.3
-
-
0.1 mM Zn2+, oxidized enzyme
6.2
-
-
0.1 mM Ca2+, reduced enzyme
7
-
-
0.1 mM Fe2+ or 0.1 mM Zn2+, reduced enzyme
9.1
-
-
0.1 mM Mn2+, reduced enzyme
63
-
Achromobacter liquidum
-
-
70.4
-
-
cloned enzyme
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8.2
-
Achromobacter liquidum
-
-
8.5
9.1
-
maximal activity between
9.3
-
-
activity assay
additional information
-
-
the activity optimum of histidase near pH 7 suggests that histidase is active predominantly in the lower, less acidic portion of the stratum corneum
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
10
-
inactive below pH 6.5, 75% of maximal activity at pH 10.0
7
10
-
pH 7.0: 10% of maximal activity, pH 10: about 50% of maximal activity
7.2
9.4
Achromobacter liquidum
-
half-maximal activity at pH 7.2 and at pH 9.4
8.1
9.9
-
50% of maximal activity at pH 8.1 and pH 9.9
additional information
-
-
-
additional information
-
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
35
-
maximal activity between
25
-
-
activity assay
50
-
Achromobacter liquidum
-
-
60
65
-
maximal activity between
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
-10
60
-
-10C: pH 9.2, assay mixture containing 21% dimethylsulfoxide remains liquid, activity is 5,8% of the activity at 30C, 60C: 20% of maximal activity
additional information
-
-
-
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
stratum corneum, skin
Manually annotated by BRENDA team
-
isoenzyme; stratum corneum; stratum granulosum
Manually annotated by BRENDA team
-
stratum granulosum
Manually annotated by BRENDA team
-
high expression level
Manually annotated by BRENDA team
-
i.e. Auerbach's plexus; intramuscular plexus
Manually annotated by BRENDA team
-
adjacent to portal triads
Manually annotated by BRENDA team
-
high expression level
Manually annotated by BRENDA team
additional information
-
grown axenically at 18C under continous illumination. Cells grown on ammonium as the sole nitrogen source contain no histidase activity, cells grown on histidine, on histidine and glycine, or on histidine and aspartate contain histidase and exhibited similar histidase activities. When the cells are grown on histidine and ammonium, or on histidine and succinate, or on histidine and glutamate, the production of histidase is slightly delayed and reaches a lower level than when cells were grown on histidine as the sole source of nitrogen. No histidase activity was detected when C. reinhardtii was grown in the presence of acetate
Manually annotated by BRENDA team
additional information
Chlamydomonas reinhardtii CCAP 11/32A
-
grown axenically at 18C under continous illumination. Cells grown on ammonium as the sole nitrogen source contain no histidase activity, cells grown on histidine, on histidine and glycine, or on histidine and aspartate contain histidase and exhibited similar histidase activities. When the cells are grown on histidine and ammonium, or on histidine and succinate, or on histidine and glutamate, the production of histidase is slightly delayed and reaches a lower level than when cells were grown on histidine as the sole source of nitrogen. No histidase activity was detected when C. reinhardtii was grown in the presence of acetate
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Anabaena variabilis (strain ATCC 29413 / PCC 7937)
Anabaena variabilis (strain ATCC 29413 / PCC 7937)
Nostoc punctiforme (strain ATCC 29133 / PCC 73102)
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
152400
-
-
gel filtration
189000
-
-
sucrose density gradient centrifugation
190000
-
-
sedimentation equilibrium
200000
-
Achromobacter liquidum
-
gel filtration
200000
-
-
sedimentation equilibrium
203000
-
-
disc gel electrophoresis
204000
-
toad
-
sucrose density gradient centrifugation
210000
-
-
sedimentation equilibrium
210000
-
-
sucrose density gradient centrifugation
210000
-
-
-
218000
-
-
sucrose density gradient centrifugation
220000
-
-
sucrose density gradient centrifugation
220000
-
-
gel-permeation chromatography, liver and epidermis enzyme
220000
-
-
gel filtration
220000
-
-
sucrose density gradient centrifugation
226000
-
-
sucrose density gradient centrifugation
243000
-
-
sucrose density gradient centrifugation
additional information
-
-
-
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 71800, SDS-PAGE
tetramer
-
4 * 55000, SDS-PAGE
tetramer
-
4 * 55675, calculation from sequence of amino acid
tetramer
-
4 * 53000, calculation from sequence of amino acid; 4 * 55000, denaturing PAGE
tetramer
-
4 * 53700, calculation from sequence of amino acid
tetramer
-
4 * 53559, calculation from sequence of amino acid
tetramer
-
homotetramer with D2-symmetry, model building
tetramer
-
-
tetramer
-
4 * 54000, sedimentation in the presence of 6 M guanidine hypochloride and mercaptoethanol
tetramer
-
-
tetramer
-
-
tetramer
-
4 * 38100, SDS-PAGE
tetramer
Bacillus subtilis Marburg 168
-
4 * 55675, calculation from sequence of amino acid
-
tetramer
Chlamydomonas reinhardtii CCAP 11/32A
-
4 * 38100, SDS-PAGE
-
tetramer
-
4 * 53700, calculation from sequence of amino acid
-
tetramer
Streptomyces griseus NRRL B-2682
-
4 * 53000, calculation from sequence of amino acid; 4 * 55000, denaturing PAGE
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
autocatalytic intrachain posttranslational cyclization
additional information
-
the peptide at the active center of the enzyme is considered to be posttranslationally dehydrated to form an electrophilic 4-methylidene-imidazole-one group
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-
Achromobacter liquidum
-
construction of enzyme structure with a closed active site by modifying the HAL structure including the L-cysteine inhibitor by replacement of the 39-80 loop containing the catalytically essential Tyr53, in every subunit of the homotetrameric enzyme. The most plausible reaction pathway involves the N-3,5-dihydro-5-methylidene-4H-imidazol-4-one intermediate structure in which the L-histidine substrate is covalently bound to the N-3,5-dihydro-5-methylidene-4H-imidazol-4-one prosthetic group of the apoenzyme via the amino group. Zn-complex formation plays a role in the reactivity and substrate specificity
-
crystal structure of C273A/D145A, C273A/F329A and C273A/F329G double mutants at 2.25 A, 2.0 A and 1.9 A resolution, respectively; crystal structure of native histidase inactivated with L-cystein at 1.0 A and Y280F mutant histidase at 1.7 A
-
structure solved to 1.8 A resolution
-
wild-type and mutant
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
75
-
Achromobacter liquidum
-
15 min, stable for 30 min, without loss of activity
80
-
-
15 min, no loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
rapid decrease of activity in presence of mercaptoethanol or cysteine, 56% of initial activity after 1 d, 20% of initial activity after 2 d. In presence of DTT, the enzyme remains stable for several days
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
in the absence of L-cysteine enzyme is completely stable in an atmosphere of N2 and O2
-
34285
inactivation of the enzyme by L-cysteine requires presence of O2
-
34285
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
5C, crystalline enzyme in 3.5 M ammonium sulfate, stable for 1 year
Achromobacter liquidum
-
37C, enzyme in solution: 50% loss of activity after 9.5 days, microencapsulated enzyme: 50% loss of activity after 15 days
-
4C, enzyme in solution: 27% loss of activity after 21 days, and 60% loss of activity after 77 days, microencapsulated enzyme: 5% loss of activity after 21 days, and less than 50% loss of activity after 77 days
-
-10C, 50% loss of activity after 4 months
-
-20C, 0.05 M potassium phosphate buffer, pH 7.0, no significant loss of activity for 2 years
-
0-4C, in a tube containing a few drops of chloroform
-
2C, 0.1 M potassium phosphate, pH 7.2, 0.1 mM MnCl2 saturated with chloroform, stable for 9 months without loss of activity
-
0C, 24 h, pH 3.0 or pH 12.0, complete loss of activity
-
0C, 24 h, pH 7.0-10.0, enzyme retains full activity
-
0C, complete loss of activity within 1 week
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-
Achromobacter liquidum
-
recombinant histidase
-
native and recombinant enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
into the pT7-7 vector for expression in Escherichia coli BL21DE3 cells
-
expression in Escherichia coli
-
expression in Escherichia coli as a His-tagged fusion protein
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
A142D
-
3.4% of wild-type activity
A142G
-
93% of wild-type activity
C273A
-
20% of wild-type kcat
C273A/D145A
-
no activity, crystal structure
C273A/E414A
-
no activity
C273A/E414Q
-
0.06% of wild-type kcat
C273A/F329A
-
0.2% of wild-type kcat
C273A/F329A
-
0.04% of wild-type activity, crystal structure
C273A/F329G
-
no activity, crystal structure
C273A/H83L
-
no activity
C273A/N195A
-
0.02% of wild-type kcat
C273A/Q277A
-
0.2% of wild-type kcat
C273A/R283I
-
0.9% of wild-type kcat
C273A/R283K
-
0.01% of wild-type kcat
C273A/Y280F
-
0.4% of wild-type kcat
C273A/Y53F
-
no activity
Cys273A
-
mutant yields rectangular crystals
D145A
-
no activity
F329A
-
0.04% of wild-type activity
F329G
-
no activity
G141A
-
1.1% of wild-type activity
G144A
-
37% of wild-type activity
Y280F
-
0.9% of wild-type activity
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystalline enzyme is prepared with 24% recovery of activity
Achromobacter liquidum
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
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enzyme can be successfully microcapsulated within cellulose nitrate artificial cells
analysis
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a potentiometric sensor is made by immobilizing histidine ammonia-lyase on an ammonia gas-sensing electrode