Histidine catabolism (Homo sapiens)

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Bibliography

1. Morris ML, Lee SC, Harper AE.; ''Influence of differential induction of histidine catabolic enzymes on histidine degradation in vivo.''; PubMed Europe PMC Scholia
2. Drozak J, Piecuch M, Poleszak O, Kozlowski P, Chrobok L, Baelde HJ, de Heer E.; ''UPF0586 Protein C9orf41 Homolog Is Anserine-producing Methyltransferase.''; PubMed Europe PMC Scholia
3. Murley LL, Mejia NR, MacKenzie RE.; ''The nucleotide sequence of porcine formiminotransferase cyclodeaminase. Expression and purification from Escherichia coli.''; PubMed Europe PMC Scholia
4. Yamauchi K, Sekizawa K, Suzuki H, Nakazawa H, Ohkawara Y, Katayose D, Ohtsu H, Tamura G, Shibahara S, Takemura M.; ''Structure and function of human histamine N-methyltransferase: critical enzyme in histamine metabolism in airway.''; PubMed Europe PMC Scholia
5. Yamada S, Ohira M, Horie H, Ando K, Takayasu H, Suzuki Y, Sugano S, Hirata T, Goto T, Matsunaga T, Hiyama E, Hayashi Y, Ando H, Suita S, Kaneko M, Sasaki F, Hashizume K, Ohnuma N, Nakagawara A.; ''Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas.''; PubMed Europe PMC Scholia
6. Hilton JF, Christensen KE, Watkins D, Raby BA, Renaud Y, de la Luna S, Estivill X, MacKenzie RE, Hudson TJ, Rosenblatt DS.; ''The molecular basis of glutamate formiminotransferase deficiency.''; PubMed Europe PMC Scholia
7. Horton JR, Sawada K, Nishibori M, Zhang X, Cheng X.; ''Two polymorphic forms of human histamine methyltransferase: structural, thermal, and kinetic comparisons.''; PubMed Europe PMC Scholia
8. Drozak J, Veiga-da-Cunha M, Vertommen D, Stroobant V, Van Schaftingen E.; ''Molecular identification of carnosine synthase as ATP-grasp domain-containing protein 1 (ATPGD1).''; PubMed Europe PMC Scholia
9. Mamune-Sato R, Yamauchi K, Tanno Y, Ohkawara Y, Ohtsu H, Katayose D, Maeyama K, Watanabe T, Shibahara S, Takishima T.; ''Functional analysis of alternatively spliced transcripts of the human histidine decarboxylase gene and its expression in human tissues and basophilic leukemia cells.''; PubMed Europe PMC Scholia
10. Rutherford K, Parson WW, Daggett V.; ''The histamine N-methyltransferase T105I polymorphism affects active site structure and dynamics.''; PubMed Europe PMC Scholia
11. Kawai Y, Moriyama A, Asai K, Coleman-Campbell CM, Sumi S, Morishita H, Suchi M.; ''Molecular characterization of histidinemia: identification of four missense mutations in the histidase gene.''; PubMed Europe PMC Scholia
12. Espinós C, Pineda M, Martínez-Rubio D, Lupo V, Ormazabal A, Vilaseca MA, Spaapen LJ, Palau F, Artuch R.; ''Mutations in the urocanase gene UROC1 are associated with urocanic aciduria.''; PubMed Europe PMC Scholia
13. Solans A, Estivill X, de la Luna S.; ''Cloning and characterization of human FTCD on 21q22.3, a candidate gene for glutamate formiminotransferase deficiency.''; PubMed Europe PMC Scholia

History

External references

DataNodes

Name	Type	Database reference	Comment
4I-5PROA	Metabolite	CHEBI:27384 (ChEBI)
ADP	Metabolite	CHEBI:456216 (ChEBI)
AMDHD1	Protein	Q96NU7 (Uniprot-TrEMBL)
ATP	Metabolite	CHEBI:30616 (ChEBI)
AdoHcy	Metabolite	CHEBI:16680 (ChEBI)
AdoMet	Metabolite	CHEBI:15414 (ChEBI)
Anserine	Metabolite	CHEBI:18323 (ChEBI)
CARN	Metabolite	CHEBI:15727 (ChEBI)
CARNMT1	Protein	Q8N4J0 (Uniprot-TrEMBL)
CARNS1	Protein	A5YM72 (Uniprot-TrEMBL)
CO2	Metabolite	CHEBI:16526 (ChEBI)
FITHF	Metabolite	CHEBI:15639 (ChEBI)
FTCD	Protein	O95954 (Uniprot-TrEMBL)
FTCD octamer	Complex	R-HSA-70908 (Reactome)
H+	Metabolite	CHEBI:15378 (ChEBI)
H2O	Metabolite	CHEBI:15377 (ChEBI)
HAL	Protein	P42357 (Uniprot-TrEMBL)
HNMT	Protein	P50135 (Uniprot-TrEMBL)
Hist	Metabolite	CHEBI:18295 (ChEBI)
L-Glu	Metabolite	CHEBI:29985 (ChEBI)
L-His	Metabolite	CHEBI:32513 (ChEBI)
MeHist	Metabolite	CHEBI:29009 (ChEBI)
NAD+	Metabolite	CHEBI:57540 (ChEBI)
NF-Glu	Metabolite	CHEBI:18327 (ChEBI)
NH4+	Metabolite	CHEBI:28938 (ChEBI)
PXLP-K305-HDC	Protein	P19113 (Uniprot-TrEMBL)
PXLP-K305-HDC dimer	Complex	R-HSA-977300 (Reactome)
Pi	Metabolite	CHEBI:43474 (ChEBI)
THF	Metabolite	CHEBI:15635 (ChEBI)
UCA	Metabolite	CHEBI:30817 (ChEBI)
UROC1	Protein	Q96N76 (Uniprot-TrEMBL)
UROC1:NAD+	Complex	R-HSA-70901 (Reactome)
b-Ala	Metabolite	CHEBI:16958 (ChEBI)

Annotated Interactions

Source	Target	Type	Database reference	Comment
	4I-5PROA	Arrow	R-HSA-70903 (Reactome)
4I-5PROA			R-HSA-70906 (Reactome)
	ADP	Arrow	R-HSA-6786245 (Reactome)
AMDHD1		mim-catalysis	R-HSA-70906 (Reactome)
ATP			R-HSA-6786245 (Reactome)
	AdoHcy	Arrow	R-HSA-175993 (Reactome)
	AdoHcy	Arrow	R-HSA-8876789 (Reactome)
AdoMet			R-HSA-175993 (Reactome)
AdoMet			R-HSA-8876789 (Reactome)
	Anserine	Arrow	R-HSA-8876789 (Reactome)
	CARN	Arrow	R-HSA-6786245 (Reactome)
CARNMT1		mim-catalysis	R-HSA-8876789 (Reactome)
CARN			R-HSA-8876789 (Reactome)
CARNS1		mim-catalysis	R-HSA-6786245 (Reactome)
	CO2	Arrow	R-HSA-977301 (Reactome)
	FITHF	Arrow	R-HSA-70920 (Reactome)
FTCD octamer		mim-catalysis	R-HSA-70920 (Reactome)
	H+	Arrow	R-HSA-70906 (Reactome)
H2O			R-HSA-70903 (Reactome)
H2O			R-HSA-70906 (Reactome)
HAL		mim-catalysis	R-HSA-70899 (Reactome)
HNMT		mim-catalysis	R-HSA-175993 (Reactome)
	Hist	Arrow	R-HSA-977301 (Reactome)
Hist			R-HSA-175993 (Reactome)
	L-Glu	Arrow	R-HSA-70920 (Reactome)
L-His			R-HSA-6786245 (Reactome)
L-His			R-HSA-70899 (Reactome)
L-His			R-HSA-977301 (Reactome)
	MeHist	Arrow	R-HSA-175993 (Reactome)
	NF-Glu	Arrow	R-HSA-70906 (Reactome)
NF-Glu			R-HSA-70920 (Reactome)
	NH4+	Arrow	R-HSA-70899 (Reactome)
PXLP-K305-HDC dimer		mim-catalysis	R-HSA-977301 (Reactome)
	Pi	Arrow	R-HSA-6786245 (Reactome)
			R-HSA-175993 (Reactome)	Histamine (Hist) plays important biological roles in cell-to-cell communication via by binding to histamine receptors and its local action is terminated primarily by methylation. Histamine is inactivated principally by two enzymes: histamine N-methyltransferase (HNMT) and diamine oxidase. HNMT uses the methyl donor AdoMet, methylates Hist to form methylhistamine (MetHist) (Yamauchi et al. 1994). The common polymorphism T105I correlates with high (T) or low (I) activity phenotypes (Horton et al. 2001, Rutherford et al. 2008).
			R-HSA-6786245 (Reactome)	Carnosine (beta-alanyl-L-histidine) and homocarnosine (gamma-aminobutyryl-L-histidine) are abundant dipeptides in skeletal muscle and brain of most vertebrates. Carnosine synthase 1 (CARNS1) transforms ATP, L-histidine (L-His) and beta-alanine (b-Ala) to carnosine (CARN) with much greater efficiency than synthesis of homocarnosine (Drozak et al. 2010).
			R-HSA-70899 (Reactome)	Cytosolic histidine ammonia lyase (HAL) catalyzes the reaction of histidine to form urocanate and NH4+ (Kawai et al. 2005).
			R-HSA-70903 (Reactome)	Cytosolic urocanate hydratase (UROC1) catalyzes the hydrolysis of urocanate to form 4-imidazolone-5-propanoate. Human UROC1 was first identified in surveys of genes differentially expressed in hepatoblastoma (Yamamda et al. 2004). Recent biochemical and molecular studies of UROC1 protein and cDNA from a patient with urocanic aciduria has confirmed the function of UROC1 in vivo (Espinos et al. 2009).
			R-HSA-70906 (Reactome)	Cytosolic imidazolonepropionase catalyzes the hydrolysis of 4-imidazolone-5-propanoate to form N-Formimino-L-glutamate. While evidence from many experimental systems indicates that this reaction occurs, existence of the human enzyme is inferred only from high-throughput screening studies (e.g., Yamada et al. 2004).
			R-HSA-70920 (Reactome)	Cytosolic formimidoyltransferase-cyclodeaminase (FTCD) catalyzes the reaction of N-formiminoglutamate and tetrahydrofolate to form glutamate and 5-formiminotetrahydrofolate. The gene encoding the human enzyme has beeen cloned and its sequence can encode a protein homologous the the biochemically characterized porcine protein (Solans et al. 2000; Murley et al. 1993). The function of FTCD in vivo was established by identification of missense mutations that reduce enzyme activity in patients with glutamate formiminotransferase deficiency (Hilton et al. 2003). Human FTCD is inferred to be an octamer by homology to the porcine enzyme (Murley et al. 1993).
			R-HSA-8876789 (Reactome)	Anserine (Beta-alanyl-N(Pi)-methyl-L-histidine) is a methylated derivative of carnosine (Beta-alanyl-L-histidine) and an abundant constituent of vertebrate skeletal muscles (Boldyrev et al. 2013). It has been suggested to serve as a proton buffer and radical scavenger. The formation of anserine is catalyzed by carnosine N-methyltransferase (CARNMT1), which transfers a methyl group from S-adenosyl-L-methionine (SAM) onto the nitrogen atom (Pi) of L-histidine residue in carnosine (Drozak et al. 2015). While CARNMT1 produces anserine in mammals, a similar reaction is catalysed by a different enzyme (carnosine N-methyltransferase 2) in birds and reptiles (Drozak et al. 2013).
			R-HSA-977301 (Reactome)	Decarboxylation of L-Histidine happens analogously to other decarboxylations of amino acids. It uses the cofactor pyridoxal phosphate and is catalyzed by histidine decarboxylase (Mamune-Sato et al, 1992).
THF			R-HSA-70920 (Reactome)
	UCA	Arrow	R-HSA-70899 (Reactome)
UCA			R-HSA-70903 (Reactome)
UROC1:NAD+		mim-catalysis	R-HSA-70903 (Reactome)
b-Ala			R-HSA-6786245 (Reactome)