The Enzyme Database

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EC 2.1.3.3     
Accepted name: ornithine carbamoyltransferase
Reaction: carbamoyl phosphate + L-ornithine = phosphate + L-citrulline
For diagram of the urea cycle and arginine biosynthesis, click here
Other name(s): citrulline phosphorylase; ornithine transcarbamylase; OTC; carbamylphosphate-ornithine transcarbamylase; L-ornithine carbamoyltransferase; L-ornithine carbamyltransferase; L-ornithine transcarbamylase; ornithine carbamyltransferase
Systematic name: carbamoyl-phosphate:L-ornithine carbamoyltransferase
Comments: The plant enzyme also catalyses the reactions of EC 2.1.3.6 putrescine carbamoyltransferase, EC 2.7.2.2 carbamate kinase and EC 3.5.3.12 agmatine deiminase, thus acting as putrescine synthase, converting agmatine [(4-aminobutyl)guanidine] and ornithine into putrescine and citrulline, respectively.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9001-69-8
References:
1.  Bishop, S.H. and Grisolia, S. Crystalline ornithine transcarbamylase. Biochim. Biophys. Acta 139 (1967) 344–348. [DOI] [PMID: 6034676]
2.  Marshall, M. and Cohen, P.P. Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. I. Isolation and subunit structure. J. Biol. Chem. 247 (1972) 1641–1653. [PMID: 4622303]
3.  Marshall, M. and Cohen, P.P. Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for carbamyl-P and L-norvaline, correlation with steady state kinetics. J. Biol. Chem. 247 (1972) 1654–1668. [PMID: 4622304]
4.  Marshall, M. and Cohen, P.P. Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. 3. Effects of chemical modifications of specific residues on ligand binding and enzymatic activity. J. Biol. Chem. 247 (1972) 1669–1682. [PMID: 4622305]
[EC 2.1.3.3 created 1961]
 
 
EC 2.1.3.6     
Accepted name: putrescine carbamoyltransferase
Reaction: carbamoyl phosphate + putrescine = phosphate + N-carbamoylputrescine
Glossary: putrescine = butane-1,4-diamine
Other name(s): PTCase; putrescine synthase; putrescine transcarbamylase
Systematic name: carbamoyl-phosphate:putrescine carbamoyltransferase
Comments: The plant enzyme also catalyses the reactions of EC 2.1.3.3 ornithine carbamoyltransferase, EC 2.7.2.2 carbamate kinase and EC 3.5.3.12 agmatine deiminase, thus acting as putrescine synthase, converting agmatine [(4-aminobutyl)guanidine] and ornithine into putrescine and citrulline, respectively.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9076-55-5
References:
1.  Roon, R.J. and Barker, H.A. Fermentation of agmatine in Streptococcus faecalis: occurrence of putrescine transcarbamoylase. J. Bacteriol. 109 (1972) 44–50. [PMID: 4621632]
2.  Srivenugopal, K.S. and Adiga, P.R. Enzymic conversion of agmatine to putrescine in Lathyrus sativus seedlings. Purification and properties of a multifunctional enzyme (putrescine synthase). J. Biol. Chem. 256 (1981) 9532–9541. [PMID: 6895223]
[EC 2.1.3.6 created 1976]
 
 
EC 2.3.1.64     
Accepted name: agmatine N4-coumaroyltransferase
Reaction: 4-coumaroyl-CoA + agmatine = CoA + N-(4-guanidinobutyl)-4-hydroxycinnamamide
Glossary: agmatine = (4-aminobutyl)guanidine
Other name(s): p-coumaroyl-CoA-agmatine N-p-coumaroyltransferase; agmatine coumaroyltransferase; 4-coumaroyl-CoA:agmatine 4-N-coumaroyltransferase
Systematic name: 4-coumaroyl-CoA:agmatine N4-coumaroyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 85030-72-4
References:
1.  Bird, C.R. and Smith, T.A. The biosynthesis of coumarylagmatine in barley seedlings. Phytochemistry 20 (1981) 2345–2346.
[EC 2.3.1.64 created 1983]
 
 
EC 2.4.2.31     
Accepted name: NAD+—protein-arginine ADP-ribosyltransferase
Reaction: NAD+ + protein L-arginine = nicotinamide + Nω-(ADP-D-ribosyl)-protein-L-arginine
Other name(s): ADP-ribosyltransferase; mono(ADP-ribosyl)transferase; NAD+:L-arginine ADP-D-ribosyltransferase; NAD(P)+-arginine ADP-ribosyltransferase; NAD(P)+:L-arginine ADP-D-ribosyltransferase; mono-ADP-ribosyltransferase; ART; ART1; ART2; ART3; ART4; ART5; ART6; ART7; NAD(P)+—protein-arginine ADP-ribosyltransferase; NAD(P)+:protein-L-arginine ADP-D-ribosyltransferase
Systematic name: NAD+:protein-L-arginine ADP-D-ribosyltransferase
Comments: Protein mono-ADP-ribosylation is a reversible post-translational modification that plays a role in the regulation of cellular activities [4]. Arginine residues in proteins act as acceptors. Free arginine, agmatine [(4-aminobutyl)guanidine], arginine methyl ester and guanidine can also do so. The enzyme from some, but not all, species can also use NADP+ as acceptor (giving rise to Nω-[(2′-phospho-ADP)-D-ribosyl]-protein-L-arginine as the product), but more slowly [1,5]. The enzyme catalyses the NAD+-dependent activation of EC 4.6.1.1, adenylate cyclase. Some bacterial enterotoxins possess similar enzymic activities. (cf. EC 2.4.2.36 NAD+—diphthamide ADP-ribosyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 81457-93-4
References:
1.  Moss, J., Stanley, S.J. and Oppenheimer, N.J. Substrate specificity and partial purification of a stereospecific NAD- and guanidine-dependent ADP-ribosyltransferase from avian erythrocytes. J. Biol. Chem. 254 (1979) 8891–8894. [PMID: 225315]
2.  Moss, J., Stanley, S.J. and Watkins, P.A. Isolation and properties of an NAD- and guanidine-dependent ADP-ribosyltransferase from turkey erythrocytes. J. Biol. Chem. 255 (1980) 5838–5840. [PMID: 6247348]
3.  Ueda, K. and Hayaishi, O. ADP-ribosylation. Annu. Rev. Biochem. 54 (1985) 73–100. [DOI] [PMID: 3927821]
4.  Corda, D. and Di Girolamo, M. Functional aspects of protein mono-ADP-ribosylation. EMBO J. 22 (2003) 1953–1958. [DOI] [PMID: 12727863]
5.  Paone, G., Stevens, L.A., Levine, R.L., Bourgeois, C., Steagall, W.K., Gochuico, B.R. and Moss, J. ADP-ribosyltransferase-specific modification of human neutrophil peptide-1. J. Biol. Chem. 281 (2006) 17054–17060. [DOI] [PMID: 16627471]
[EC 2.4.2.31 created 1984, modified 1990, modified 2006]
 
 
EC 2.5.1.104     
Accepted name: N1-aminopropylagmatine synthase
Reaction: S-adenosyl 3-(methylsulfanyl)propylamine + agmatine = S-methyl-5′-thioadenosine + N1-(3-aminopropyl)agmatine
For diagram of spermidine biosynthesis, click here
Glossary: S-adenosyl 3-(methylsulfanyl)propylamine = (3-aminopropyl){[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}methylsulfonium
Other name(s): agmatine/cadaverine aminopropyl transferase; ACAPT; PF0127 (gene name); triamine/agmatine aminopropyltransferase; SpeE (ambiguous); agmatine aminopropyltransferase; S-adenosyl 3-(methylthio)propylamine:agmatine 3-aminopropyltransferase
Systematic name: S-adenosyl 3-(methylsulfanyl)propylamine:agmatine 3-aminopropyltransferase
Comments: The enzyme is involved in the biosynthesis of spermidine from agmatine in some archaea and bacteria. The enzyme from the Gram-negative bacterium Thermus thermophilus accepts agmatine, spermidine and norspermidine with similar catalytic efficiency. The enzymes from the archaea Pyrococcus furiosus and Thermococcus kodakarensis prefer agmatine, but can utilize cadaverine, putrescine and propane-1,3-diamine with much lower catalytic efficiency. cf. EC 2.5.1.16, spermidine synthase, and EC 2.5.1.23, sym-norspermidine synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ohnuma, M., Terui, Y., Tamakoshi, M., Mitome, H., Niitsu, M., Samejima, K., Kawashima, E. and Oshima, T. N1-aminopropylagmatine, a new polyamine produced as a key intermediate in polyamine biosynthesis of an extreme thermophile, Thermus thermophilus. J. Biol. Chem. 280 (2005) 30073–30082. [DOI] [PMID: 15983049]
2.  Cacciapuoti, G., Porcelli, M., Moretti, M.A., Sorrentino, F., Concilio, L., Zappia, V., Liu, Z.J., Tempel, W., Schubot, F., Rose, J.P., Wang, B.C., Brereton, P.S., Jenney, F.E. and Adams, M.W. The first agmatine/cadaverine aminopropyl transferase: biochemical and structural characterization of an enzyme involved in polyamine biosynthesis in the hyperthermophilic archaeon Pyrococcus furiosus. J. Bacteriol. 189 (2007) 6057–6067. [DOI] [PMID: 17545282]
3.  Morimoto, N., Fukuda, W., Nakajima, N., Masuda, T., Terui, Y., Kanai, T., Oshima, T., Imanaka, T. and Fujiwara, S. Dual biosynthesis pathway for longer-chain polyamines in the hyperthermophilic archaeon Thermococcus kodakarensis. J. Bacteriol. 192 (2010) 4991–5001. [DOI] [PMID: 20675472]
4.  Ohnuma, M., Ganbe, T., Terui, Y., Niitsu, M., Sato, T., Tanaka, N., Tamakoshi, M., Samejima, K., Kumasaka, T. and Oshima, T. Crystal structures and enzymatic properties of a triamine/agmatine aminopropyltransferase from Thermus thermophilus. J. Mol. Biol. 408 (2011) 971–986. [DOI] [PMID: 21458463]
[EC 2.5.1.104 created 2013]
 
 
EC 2.7.2.2     
Accepted name: carbamate kinase
Reaction: ATP + NH3 + hydrogencarbonate = ADP + carbamoyl phosphate + H2O (overall reaction)
(1a) ATP + carbamate = ADP + carbamoyl phosphate
(1b) NH3 + hydrogencarbonate = carbamate + H2O (spontaneous)
For diagram of AMP catabolism, click here
Other name(s): CKase; carbamoyl phosphokinase; carbamyl phosphokinase
Systematic name: ATP:carbamate phosphotransferase
Comments: The enzyme catalyses the reversible conversion of carbamoyl phosphate and ADP to ATP and carbamate, which hydrolyses to ammonia and hydrogencarbonate. The physiological role of the enzyme is to generate ATP.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9026-69-1
References:
1.  Jones, M.E., Spector, L. and Lipmann, F. Carbamyl phosphate, the carbamyl donor in enzymatic citrulline synthesis. J. Am. Chem. Soc. 77 (1955) 819–820.
2.  Davis, R.H. Carbamyl phosphate synthesis in Neurospora crassa. I. Preliminary characterization of arginine-specific carbamyl phosphokinase. Biochim. Biophys. Acta 107 (1965) 44–53. [DOI] [PMID: 5857367]
3.  Glasziou, K.T. The metabolism of arginine in Serratia marcescens. II. Carbamyladenosine diphosphate phosphoferase. Aust. J. Biol. Sci. 9 (1956) 253–262.
4.  Bishop, S.H. and Grisolia, S. Crystalline carbamate kinase. Biochim. Biophys. Acta 118 (1966) 211–215. [PMID: 4959296]
5.  Srivenugopal, K.S. and Adiga, P.R. Enzymic conversion of agmatine to putrescine in Lathyrus sativus seedlings. Purification and properties of a multifunctional enzyme (putrescine synthase). J. Biol. Chem. 256 (1981) 9532–9541. [PMID: 6895223]
[EC 2.7.2.2 created 1961, modified 2018]
 
 
EC 2.7.3.10     
Accepted name: agmatine kinase
Reaction: ATP + agmatine = ADP + N4-phosphoagmatine
Glossary: agmatine = (4-aminobutyl)guanidine
Other name(s): phosphagen phosphokinase; ATP:agmatine 4-N-phosphotransferase
Systematic name: ATP:agmatine N4-phosphotransferase
Comments: L-Arginine can act as acceptor, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9076-75-9
References:
1.  Piccinni, E. and Coppellotti, O. Phosphagens in protozoa. II. Presence of phosphagen kinase in Ochramonas danica. Comp. Biochem. Physiol. 62B (1979) 287–289.
[EC 2.7.3.10 created 1984]
 
 
EC 3.5.1.40     
Accepted name: acylagmatine amidase
Reaction: benzoylagmatine + H2O = benzoate + agmatine
Glossary: agmatine = (4-aminobutyl)guanidine
Other name(s): acylagmatine amidohydrolase; acylagmatine deacylase
Systematic name: benzoylagmatine amidohydrolase
Comments: Also acts on acetylagmatine, propanoylagmatine and bleomycin B2
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 39419-74-4
References:
1.  Umezawa, H., Takahashi, Y., Fujii, A., Saino, T., Shirai, T. and Takita, T. Preparation of bleomycinic acid. Hydrolysis of bleomycin B2 by a Fusarium acylagmatine amidohydrolase. J. Antibiot. 26 (1974) 117–119. [PMID: 4131159]
[EC 3.5.1.40 created 1976]
 
 
EC 3.5.3.11     
Accepted name: agmatinase
Reaction: agmatine + H2O = putrescine + urea
For diagram of arginine catabolism, click here
Glossary: agmatine = (4-aminobutyl)guanidine
putrescine = butane-1,4-diamine
Other name(s): agmatine ureohydrolase; SpeB
Systematic name: agmatine amidinohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37289-16-0
References:
1.  Hirshfeld, I.N., Rosenfeld, H.J., Leifer, Z. and Maas, W.K. Isolation and characterization of a mutant of Escherichia coli blocked in the synthesis of putrescine. J. Bacteriol. 101 (1970) 725–730. [PMID: 4908780]
2.  Vicente, C. and Legaz, M.E. Preparation and properties of agmatine amidinohydrolase of Evernia prunastri. Physiol. Plant. 55 (1982) 335–339.
[EC 3.5.3.11 created 1972]
 
 
EC 3.5.3.12     
Accepted name: agmatine deiminase
Reaction: agmatine + H2O = N-carbamoylputrescine + NH3
Glossary: agmatine = (4-aminobutyl)guanidine
Other name(s): agmatine amidinohydrolase
Systematic name: agmatine iminohydrolase
Comments: The plant enzyme also catalyses the reactions of EC 2.1.3.3 (ornithine carbamoyltransferase), EC 2.1.3.6 (putrescine carbamoyltransferase) and EC 2.7.2.2 (carbamate kinase), thus functioning as a putrescine synthase, converting agmatine and ornithine into putrescine and citrulline, respectively.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37289-17-1
References:
1.  Smith, T.A. Agmatine iminohydrolase in maize. Phytochemistry 8 (1969) 2111–2117.
2.  Srivenugopal, K.S. and Adiga, P.R. Enzymic conversion of agmatine to putrescine in Lathyrus sativus seedlings. Purification and properties of a multifunctional enzyme (putrescine synthase). J. Biol. Chem. 256 (1981) 9532–9541. [PMID: 6895223]
[EC 3.5.3.12 created 1972]
 
 
EC 3.5.3.20     
Accepted name: diguanidinobutanase
Reaction: 1,4-diguanidinobutane + H2O = agmatine + urea
Glossary: agmatine = (4-aminobutyl)guanidine
Systematic name: 1,4-diguanidinobutane amidinohydrolase
Comments: Other diguanidinoalkanes with 3 to 10 methylene groups can also act, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 125268-65-7
References:
1.  Yorifuji, T., Kaneoke, M., Shimizu, E., Shiota, K. and Matsuo, R. Degradation of α,ω-diguanidinoalkanes and a novel enzyme, diguanidinobutane amidohydrolase, in Pseudomonas putida. Agric. Biol. Chem. 53 (1989) 3003–3009.
[EC 3.5.3.20 created 1992]
 
 
EC 3.5.3.24     
Accepted name: N1-aminopropylagmatine ureohydrolase
Reaction: N1-aminopropylagmatine + H2O = spermidine + urea
For diagram of spermidine biosynthesis, click here
Systematic name: N1-aminopropylagmatine amidinohydrolase
Comments: The enzyme, which has been characterized from the hyperthermophilic archaeon Pyrococcus kodakarensis and the thermophilic Gram-negative bacterium Thermus thermophilus, is involved in the biosynthesis of spermidine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ohnuma, M., Terui, Y., Tamakoshi, M., Mitome, H., Niitsu, M., Samejima, K., Kawashima, E. and Oshima, T. N1-aminopropylagmatine, a new polyamine produced as a key intermediate in polyamine biosynthesis of an extreme thermophile, Thermus thermophilus. J. Biol. Chem. 280 (2005) 30073–30082. [DOI] [PMID: 15983049]
2.  Morimoto, N., Fukuda, W., Nakajima, N., Masuda, T., Terui, Y., Kanai, T., Oshima, T., Imanaka, T. and Fujiwara, S. Dual biosynthesis pathway for longer-chain polyamines in the hyperthermophilic archaeon Thermococcus kodakarensis. J. Bacteriol. 192 (2010) 4991–5001. [DOI] [PMID: 20675472]
[EC 3.5.3.24 created 2013]
 
 
EC 4.1.1.19     
Accepted name: arginine decarboxylase
Reaction: L-arginine = agmatine + CO2
For diagram of arginine catabolism, click here
Glossary: agmatine = (4-aminobutyl)guanidine
Other name(s): SpeA; L-arginine carboxy-lyase
Systematic name: L-arginine carboxy-lyase (agmatine-forming)
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-77-5
References:
1.  Blethen, S.L., Boeker, E.A. and Snell, E.E. Arginine decarboxylase from Escherichia coli. I. Purification and specificity for substrates and coenzyme. J. Biol. Chem. 243 (1968) 1671–1677. [PMID: 4870599]
2.  Ramakrishna, S. and Adiga, P.R. Arginine decarboxylase from Lathyrus sativus seedlings. Purification and properties. Eur. J. Biochem. 59 (1975) 377–386. [DOI] [PMID: 1252]
3.  Taylor, E.S. and Gale, E.F. Studies on bacterial amino-acid decarboxylases. 6. Codecarboxylase content and action of inhibitors. Biochem. J. 39 (1945) 52–58. [PMID: 16747854]
[EC 4.1.1.19 created 1961]
 
 
EC 6.3.4.22     
Accepted name: tRNAIle2-agmatinylcytidine synthase
Reaction: ATP + agmatine + [tRNAIle2]-cytidine34 + H2O = [tRNAIle2]-2-agmatinylcytidine34 + AMP + 2 phosphate
Other name(s): TiaS; AF2259; tRNAIle-2-agmatinylcytidine synthetase; tRNAIle-agm2C synthetase; tRNAIle-agmatidine synthetase
Systematic name: agmatine:[tRNAIle]-cytidine34 ligase
Comments: The enzyme from the archaeon Archaeoglobus fulgidus modifies the wobble base of the CAU anticodon of the archaeal tRNAIle2 at the oxo group in position 2 of cytidine34. This modification is crucial for accurate decoding of the genetic code. In bacteria EC 6.3.4.19, tRNAIle-lysidine synthase, catalyses the modification of [tRNAIle2]-cytidine34 to [tRNAIle2]-lysidine34 .
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ikeuchi, Y., Kimura, S., Numata, T., Nakamura, D., Yokogawa, T., Ogata, T., Wada, T., Suzuki, T. and Suzuki, T. Agmatine-conjugated cytidine in a tRNA anticodon is essential for AUA decoding in archaea. Nat. Chem. Biol. 6 (2010) 277–282. [DOI] [PMID: 20139989]
2.  Terasaka, N., Kimura, S., Osawa, T., Numata, T. and Suzuki, T. Biogenesis of 2-agmatinylcytidine catalyzed by the dual protein and RNA kinase TiaS. Nat. Struct. Mol. Biol. 18 (2011) 1268–1274. [DOI] [PMID: 22002222]
3.  Osawa, T., Inanaga, H., Kimura, S., Terasaka, N., Suzuki, T. and Numata, T. Crystallization and preliminary X-ray diffraction analysis of an archaeal tRNA-modification enzyme, TiaS, complexed with tRNA(Ile2) and ATP. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67 (2011) 1414–1416. [DOI] [PMID: 22102245]
[EC 6.3.4.22 created 2013]
 
 


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