The Enzyme Database

Your query returned 4 entries.    printer_iconPrintable version



EC 2.1.1.317     
Accepted name: sphingolipid C9-methyltransferase
Reaction: S-adenosyl-L-methionine + a (4E,8E)-sphinga-4,8-dienine ceramide = S-adenosyl-L-homocysteine + a 9-methyl-(4E,8E)-sphinga-4,8-dienine ceramide
Systematic name: S-adenosyl-L-methionine:(4E,8E)-sphinga-4,8-dienine ceramide C-methyltransferase
Comments: The enzyme, characterized from the fungi Komagataella pastoris and Fusarium graminearum, acts only on ceramides and has no activity with free sphingoid bases or glucosylceramides.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ternes, P., Sperling, P., Albrecht, S., Franke, S., Cregg, J.M., Warnecke, D. and Heinz, E. Identification of fungal sphingolipid C9-methyltransferases by phylogenetic profiling. J. Biol. Chem. 281 (2006) 5582–5592. [DOI] [PMID: 16339149]
2.  Ramamoorthy, V., Cahoon, E.B., Thokala, M., Kaur, J., Li, J. and Shah, D.M. Sphingolipid C-9 methyltransferases are important for growth and virulence but not for sensitivity to antifungal plant defensins in Fusarium graminearum. Eukaryot Cell 8 (2009) 217–229. [DOI] [PMID: 19028992]
[EC 2.1.1.317 created 2015]
 
 
EC 2.1.1.340     
Accepted name: 3-aminomethylindole N-methyltransferase
Reaction: 2 S-adenosyl-L-methionine + 3-(aminomethyl)indole = 2 S-adenosyl-L-homocysteine + gramine (overall reaction)
(1a) S-adenosyl-L-methionine + 3-(aminomethyl)indole = S-adenosyl-L-homocysteine + (1H-indol-3-yl)-N-methylmethanamine
(1b) S-adenosyl-L-methionine + (1H-indol-3-yl)-N-methylmethanamine = S-adenosyl-L-homocysteine + gramine
For diagram of gramine biosynthesis, click here
Glossary: 3-(aminomethyl)indole = (1H-indol-3-yl)methanamine
gramine = (1H-indol-3-ylmethyl)dimethylamine = (1H-indol-3-yl)-N,N-dimethylmethanamine
Other name(s): NMT (gene name)
Systematic name: S-adenosyl-L-methionine:3-(aminomethyl)indole N-methyltransferase (gramine-forming)
Comments: The enzyme, characterized from Hordeum vulgare (barley), catalyses two successive N-methylation reactions during the biosynthesis of gramine, a toxic indole alkaloid.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Leland, T.J. and Hanson, A.D. Induction of a specific N-methyltransferase enzyme by long-term heat stress during barley leaf growth. Plant Physiol. 79 (1985) 451–457. [PMID: 16664431]
2.  Larsson, K.A., Zetterlund, I., Delp, G. and Jonsson, L.M. N-Methyltransferase involved in gramine biosynthesis in barley: cloning and characterization. Phytochemistry 67 (2006) 2002–2008. [DOI] [PMID: 16930646]
[EC 2.1.1.340 created 2017]
 
 
EC 2.6.1.80     
Accepted name: nicotianamine aminotransferase
Reaction: nicotianamine + 2-oxoglutarate = 3′′-deamino-3′′-oxonicotianamine + L-glutamate
For diagram of nicotianamine biosynthesis, click here
Other name(s): NAAT; NAAT-I; NAAT-II; NAAT-III; nicotianamine transaminase
Systematic name: nicotianamine:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. This enzyme is produced by grasses. They secrete both the nicotianamine and the transaminated product into the soil around them. Both compounds chelate iron(II) and iron(III); these chelators, called mugineic acid family phytosiderophores, are taken up by the grass, which is thereby supplied with iron.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 154907-64-9
References:
1.  Kanazawa, K., Higuchi, K., Nishizawa, N.-K., Fushiya, S., Chino, M. and Mori, S. Nicotianamine aminotransferase activities are correlated with the phytosiderophore secretions under Fe-deficient conditions in Gramineae. J. Exp. Bot. 45 (1994) 1903–1906.
2.  Takahashi, M., Yamaguchi, H., Nakanishi, H., Shioiri, T., Nishizawa, N.K. and Mori, S. Cloning two genes for nicotianamine aminotransferase, a critical enzyme in iron acquisition (Strategy II) in graminaceous plants. Plant Physiol. 121 (1999) 947–956. [PMID: 10557244]
3.  Schaaf, G., Ludewig, U., Erenoglu, B.E., Mori, S., Kitahara, T. and von Wirén, N. ZmYS1 functions as a proton-coupled symporter for phytosideorophore- and nicotianamine-chelated metals. J. Biol. Chem. 279 (2004) 9091–9096. [DOI] [PMID: 14699112]
[EC 2.6.1.80 created 2005]
 
 
EC 4.1.2.8     
Accepted name: indole-3-glycerol-phosphate lyase
Reaction: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate
For diagram of reaction, click here
Other name(s): tryptophan synthase α; TSA; indoleglycerolphosphate aldolase; indole glycerol phosphate hydrolase; indole synthase; indole-3-glycerolphosphate D-glyceraldehyde-3-phosphate-lyase; indole-3-glycerol phosphate lyase; IGL; BX1; (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate D-glyceraldehyde-3-phosphate-lyase
Systematic name: (1S,2R)-1-C-(indol-3-yl)glycerol-3-phosphate D-glyceraldehyde-3-phosphate-lyase (indole-forming)
Comments: Forms part of the defence mechanism against insects and microbial pathogens in the grass family, Gramineae, where it catalyses the first committed step in the formation of the cyclic hydroxamic acids 2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one (DIBOA) and 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one (DIMBOA) [1]. This enzyme resembles the α-subunit of EC 4.2.1.20, tryptophan synthase [3], for which, (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate is also a substrate, but, unlike tryptophan synthase, its activity is independent of the β-subunit and free indole is released [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9014-52-2
References:
1.  Yanofsky, C. The enzymatic conversion of anthranilic acid to indole. J. Biol. Chem. 223 (1956) 171–184. [PMID: 13376586]
2.  Frey, M., Chomet, P., Glawischnig, E., Stettner, C., Grün, S., Winklmair, A., Eisenreich, W., Bacher, A., Meeley, R.B., Briggs, S.P., Simcox, K. and Gierl, A. Analysis of a chemical plant defense mechanism in grasses. Science 277 (1997) 696–699. [DOI] [PMID: 9235894]
3.  Frey, M., Stettner, C., Paré, P.W., Schmelz, E.A., Tumlinson, J.H. and Gierl, A. An herbivore elicitor activates the gene for indole emission in maize. Proc. Natl. Acad. Sci. USA 97 (2000) 14801–14806. [DOI] [PMID: 11106389]
4.  Melanson, D., Chilton, M.D., Masters-Moore, D. and Chilton, W.S. A deletion in an indole synthase gene is responsible for the DIMBOA-deficient phenotype of bxbx maize. Proc. Natl. Acad. Sci. USA 94 (1997) 13345–13350. [DOI] [PMID: 9371848]
[EC 4.1.2.8 created 1961, deleted 1972, reinstated 2006]
 
 


Data © 2001–2020 IUBMB
Web site © 2005–2020 Andrew McDonald