Agmatinase

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Agmatinase

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agmatinase

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In enzymology, an agmatinase (EC 3.5.3.11) is an enzyme that catalyzes the chemical reaction

agmatine + H₂O $\rightleftharpoons$ putrescine + urea

Thus, the two substrates of this enzyme are agmatine and H₂O, whereas its two products are putrescine and urea.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is agmatine amidinohydrolase. Other names in common use include agmatine ureohydrolase, and SpeB. This enzyme participates in urea cycle and metabolism of amino groups.

Genetics

Agmatine ureohydrolase (agmatinase)

Identifiers

Symbols

AGMAT; FLJ23384

External IDs

MGI: 1923236 HomoloGene: 99855 GeneCards: AGMAT Gene

EC number

3.5.3.11

Gene Ontology
Molecular function	• agmatinase activity • hydrolase activity • metal ion binding
Cellular component	• mitochondrion
Biological process	• polyamine metabolic process • spermidine biosynthetic process • putrescine biosynthetic process • cellular nitrogen compound metabolic process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

n/a

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
15.9 – 15.91 Mb

Chr 4:
141.3 – 141.32 Mb

PubMed search

[1]

[2]

In humans, the enzyme is encoded by the AGMAT gene.^[1]^[2]^[3]^[4]

Structural studies

As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1GQ6, 1GQ7, 1WOG, 1WOH, and 1WOI.

References

^ Mistry SK, Burwell TJ, Chambers RM, Rudolph-Owen L, Spaltmann F, Cook WJ, Morris SM Jr (Jan 2002). "Cloning of human agmatinase. An alternate path for polyamine synthesis induced in liver by hepatitis B virus". Am J Physiol Gastrointest Liver Physiol 282 (2): G375–81. doi:10.1152/ajpgi.00386.2001. PMID 11804860.
^ Dallmann K, Junker H, Balabanov S, Zimmermann U, Giebel J, Walther R (Dec 2003). "Human agmatinase is diminished in the clear cell type of renal cell carcinoma". Int J Cancer 108 (3): 342–7. doi:10.1002/ijc.11459. PMID 14648699.
^ Iyer RK, Kim HK, Tsoa RW, Grody WW, Cederbaum SD (Mar 2002). "Cloning and characterization of human agmatinase". Mol Genet Metab 75 (3): 209–18. doi:10.1006/mgme.2001.3277. PMID 11914032.
^ "Entrez Gene: AGMAT agmatine ureohydrolase (agmatinase)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=79814.

Morris SM (2004). "Vertebrate agmatinases: what role do they play in agmatine catabolism?". Ann. N. Y. Acad. Sci. 1009: 30–3. doi:10.1196/annals.1304.003. PMID 15028567.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Chen FW, Davies JP, Ioannou YA (1998). "Differential gene expression in apoptosis: identification of ribosomal protein 23K, a cell proliferation inhibitor". Mol. Genet. Metab. 64 (4): 271–82. doi:10.1006/mgme.1998.2718. PMID 9758718.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
Kim KH, Ahn HJ, Kim DJ, et al. (2006). "Expression, crystallization and preliminary X-ray crystallographic analysis of human agmatinase". Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 61 (Pt 10): 889–91. doi:10.1107/S1744309105027193. PMC 1991308. PMID 16511187. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1991308.
Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414.
Hirshfield IN, Rosenfeld HJ, Leifer Z, Maas WK (1970). "Isolation and Characterization of a Mutant of Escherichia coli Blocked in the Synthesis of Putrescine". J. Bacteriol. 101 (3): 725–30. PMC 250384. PMID 4908780. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=250384.
Vicente C and Legaz ME (1982). "Preparation and properties of agmatine amidinohydrolase of Evernia prunastri". Physiol. Plant. 55: 335–339.
MeSH agmatinase

v · d · eHydrolases: carbon-nitrogen non-peptide (EC 3.5)

3.5.1: Linear amides / Amidohydrolases	Asparaginase · Glutaminase · Urease · Biotinidase · Aspartoacylase · Ceramidase · Aspartylglucosaminidase · Fatty acid amide hydrolase · Histone deacetylase (Sirtuin)

3.5.2: Cyclic amides/ Amidohydrolases	Barbiturase · Beta-lactamase

3.5.3: Linear amidines/ Ureohydrolases	Arginase · Agmatinase · Protein-arginine deiminase

3.5.4: Cyclic amidines/ Aminohydrolases	Guanine deaminase · Adenosine deaminase · AMP deaminase · Inosine monophosphate synthase · DCMP deaminase · GTP cyclohydrolase I · Cytidine deaminase (AICDA, Activation-Induced (Cytidine) Deaminase)

3.5.5: Nitriles/ Aminohydrolases	Nitrilase

3.5.99: Other	Riboflavinase · Thiaminase II

B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6

Metabolism: amino acid metabolism · synthesis and catabolism enzymes (essential in CAPS)

K→acetyl-CoA

G→pyruvate
→citrate

glycine→serine→	Serine hydroxymethyltransferase · Serine dehydratase glycine→creatine: Guanidinoacetate N-methyltransferase · Creatine kinase

alanine→	Alanine transaminase

cysteine→	D-cysteine desulfhydrase

threonine→	L-threonine dehydrogenase

G→glutamate→
α-ketoglutarate

G→propionyl-CoA→
succinyl-CoA

VALINE→	Branched chain aminotransferase · Branched-chain alpha-keto acid dehydrogenase complex · Enoyl-CoA hydratase · 3-hydroxyisobutyryl-CoA hydrolase · 3-hydroxyisobutyrate dehydrogenase · Methylmalonate semialdehyde dehydrogenase

ISOLEUCINE→	Branched chain aminotransferase · Branched-chain alpha-keto acid dehydrogenase complex · 3-hydroxy-2-methylbutyryl-CoA dehydrogenase

METHIONINE→	generation of homocysteine: Methionine adenosyltransferase · Adenosylhomocysteinase regeneration of methionine: Methionine synthase/Homocysteine methyltransferase · Betaine-homocysteine methyltransferase conversion to cysteine: Cystathionine beta synthase · Cystathionine gamma-lyase

THREONINE→	Threonine aldolase

→succinyl-CoA→TCA	Propionyl-CoA carboxylase · Methylmalonyl CoA epimerase · Methylmalonyl-CoA mutase

G→fumarate


PHENYLALANINE→tyrosine→	Phenylalanine hydroxylase · Tyrosine aminotransferase · 4-Hydroxyphenylpyruvate dioxygenase · Homogentisate 1,2-dioxygenase · Fumarylacetoacetate hydrolase tyrosine→melanin: Tyrosinase

G→oxaloacetate


asparagine→aspartate→	Asparaginase/Asparagine synthetase · Aspartate transaminase

M: MET

mt, k, c/g/r/p/y/i, f/h/s/l/o/e, a/u, n, m

k, cgrp/y/i, f/h/s/l/o/e, au, n, m, epon

m(A16/C10),i(k, c/g/r/p/y/i, f/h/s/o/e, a/u, n, m)

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