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Information on EC 4.3.1.3 - histidine ammonia-lyase and Organism(s) Homo sapiens

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EC Tree
     4 Lyases
         4.3 Carbon-nitrogen lyases
             4.3.1 Ammonia-lyases
                4.3.1.3 histidine ammonia-lyase
IUBMB Comments
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 . This unique cofactor is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine . This enzyme catalyses the first step in the degradation of histidine and the product, urocanic acid, is further metabolized to glutamate [2,3].
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Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
hal, histidase, histidine ammonia-lyase, histidine ammonia lyase, histidinase, l-histidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ammonia-lyase, histidine
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-
-
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histidase
histidase, Hut
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-
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histidinase
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-
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histidine alpha-deaminase
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-
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histidine ammonia lyase
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histidine ammonia-lyase
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histidine deaminase
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-
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L-HAL
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-
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L-histidase
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-
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L-histidine NH3-lyase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-histidine = urocanate + NH3
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Deamination
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elimination of NH3
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-
PATHWAY SOURCE
PATHWAYS
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-, -, -, -
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].
CAS REGISTRY NUMBER
COMMENTARY hide
9013-75-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-histidine
trans-urocanic acid + NH3
show the reaction diagram
L-histidine
urocanate + NH3
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-histidine
trans-urocanic acid + NH3
show the reaction diagram
L-histidine
urocanate + NH3
show the reaction diagram
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-
-
r
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
all-trans retinoic acid
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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
interleukin-1alpha
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treatment of IL-1a reduces histidase expression, the suppressive effect can be reverted by concomitant treatment with interleukin-1alpha receptor antagonist
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TGF-alpha
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most pronounced effect, leads to almost complete suppression of histidase expression
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TNF-alpha
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suppresses the expression of histidase
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
estrogen
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transcriptional activator of histidase expression
glucocorticoid
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transcriptional activator of histidase expression
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additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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epidermal
Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HUTH_HUMAN
657
0
72698
Swiss-Prot
other Location (Reliability: 3)
Q2PH55_HUMAN
49
0
4975
TrEMBL
other Location (Reliability: 3)
Q2PH58_HUMAN
41
0
4547
TrEMBL
Secretory Pathway (Reliability: 4)
Q2PH61_HUMAN
46
0
5147
TrEMBL
other Location (Reliability: 2)
Q2PH60_HUMAN
41
0
4590
TrEMBL
Mitochondrion (Reliability: 5)
Q2PH59_HUMAN
41
0
4534
TrEMBL
other Location (Reliability: 4)
Q2PH56_HUMAN
46
0
4745
TrEMBL
other Location (Reliability: 3)
Q2PH57_HUMAN
46
0
4761
TrEMBL
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
243000
-
sucrose density gradient centrifugation
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
autocatalytic intrachain posttranslational cyclization
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
brefeldin A induces expression strongly
increased expression is observed in Hep-G2 cells treated with Vemurafenib
SU11274 and ATM kinase inhibitor increase expression slightly
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hanson, K.R.; Havir, E.A.
The enzymic elimination of ammonia
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
7
75-166
1972
Klebsiella aerogenes, Bacillus subtilis, Comamonas testosteroni, Homo sapiens, Pseudomonas sp., Pseudomonas aeruginosa, Pseudomonas fluorescens, Rattus norvegicus, Salmonella enterica subsp. enterica serovar Typhimurium, toad, Pseudomonas fluorescens A.3.12
-
Manually annotated by BRENDA team
Hassall, H.
Use of L-histidine ammonia-lyase for the determination of L-histidine
Methods Enzymol.
17B
895-897
1971
Homo sapiens, Pseudomonas sp., Pseudomonas putida
-
Manually annotated by BRENDA team
La Du, B.N.
L-Histidine ammonia-lyase (human stratum corneum)
Methods Enzymol.
17B
891-894
1971
Homo sapiens
-
Manually annotated by BRENDA team
Donnelly, M.; Fedeles, F.; Wirstam, M.; Siegbahn, P.E.; Zimmer, M.
Computational analysis of the autocatalytic posttranslational cyclization observed in histidine ammonia-lyase. A comparison with green fluorescent protein
J. Am. Chem. Soc.
123
4679-4686
2001
Homo sapiens
Manually annotated by BRENDA team
Kawai, Y.; Moriyama, A.; Asai, K.; Coleman-Campbell, C.M.; Sumi, S.; Morishita, H.; Suchi, M.
Molecular characterization of histidinemia: identification of four missense mutations in the histidase gene
Hum. Genet.
116
340-346
2005
Homo sapiens
Manually annotated by BRENDA team
Welsh, M.M.; Karagas, M.R.; Applebaum, K.M.; Spencer, S.K.; Perry, A.E.; Nelson, H.H.
A role for ultraviolet radiation immunosuppression in non-melanoma skin cancer as evidenced by gene-environment interactions
Carcinogenesis
29
1950-1954
2008
Homo sapiens
Manually annotated by BRENDA team
Eckhart, L.; Schmidt, M.; Mildner, M.; Mlitz, V.; Abtin, A.; Ballaun, C.; Fischer, H.; Mrass, P.; Tschachler, E.
Histidase expression in human epidermal keratinocytes: regulation by differentiation status and all-trans retinoic acid
J. Dermatol. Sci.
50
209-215
2008
Homo sapiens
Manually annotated by BRENDA team
Yamaguchi, K.; Zhu, C.; Ohsugi, T.; Yamaguchi, Y.; Ikenoue, T.; Furukawa, Y.
Bidirectional reporter assay using HAL promoter and TOPFLASH improves specificity in high-throughput screening of Wnt inhibitors
Biotechnol. Bioeng.
114
2868-2882
2017
Homo sapiens (P42357)
Manually annotated by BRENDA team