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Information on EC 4.3.1.3 - histidine ammonia-lyase and Organism(s) Homo sapiens and UniProt Accession P42357

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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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This record set is specific for:
Homo sapiens
UNIPROT: P42357
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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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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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L-HAL
-
-
-
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L-histidase
-
-
-
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L-histidine NH3-lyase
-
-
-
-
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
-
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
-
-
-
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
-
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
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SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
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)
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