Enzyme Handbook 11 Springer-Verlag Berlin Heidelberg GmbH
Attention all "Enzyme Handbook" users:
A file with the complete volume indexes Vols. 1 through 11 in delimited ASCII format is available for downloading at no charge from the Springer EARN mailbox. Delimited ASCII format can be imported into most databanks.
The file has been compressed using the popular shareware program "PKZIP" (Trademark of PKware Inc., PKZIP is available from most BBS and shareware distributors).
This file is distributed without any expressed or implied warranty.
To receive this file send an e-mail message to: SVSERV@DHDSPRI6. BITNET
The message must be: GET /CHEMISTRY/ENZ_HB.ZIP
SVSERV is an automatic data distribution system. It responds to your message. The following commands are available:
HELP DIR (name) INDEX (name) CD <name> SEND <filename> GET <filename>
returns a detailed instruction set for the use of SVSER\1, returns a list of files available in the directory "name", same as "DIR" changes to directory "name", invokes a message with the file "filename", same as "SEND".
D. Schomburg · D. Stephan (Eds.) GBF- Gesellschaft tor Biotechnologische Forschung
Enzyme Handbook Class 2.1 - 2.3 Transferases 11 EC 2.1 - EC 2.3.1
for EC 2.3.2 see Vol. 12
Professor Dr. Dietmar Schomburg Dr. Dorte Stephan
GBF- Gesellschaft fOr Biotechnologische Forschung mbH Mascheroder Weg 1
38124 Braunschweig FRG
This collection of datasheets was generated from the database ,BRENDA"
ISBN 978-3-642-4 7806-2
Die Deutsche Bibliothek- CIP-Einheitsaufnahme
Enzyme handbook: [this collection of datasheets was generated from the database "BRENDA"]/GBF, Gesellschaft fUr Biotechnologische Forschung. D. Schomburg; D. Stephan (ed.}.- Berlin; Heidelberg; New York; London; Paris; Tokyo; Hong Kong; Barcelona; Budapest: Springer. NE: Schomburg, Dietmar [Hrsg.]; Gesellschaft fUr Biotechnologische Forschung (Braunschweig)
11. Class 2.1 - 2.3: Transferases. - 1996
ISBN 978-3-642-47806-2 ISBN 978-3-642-61030-1 (eBook) DOI 10.1007/978-3-642-61030-1
This work is subject to copyright. All rights are reserved, whether the whole or part of the material is concerned, specifically the rights of translation, reprinting, reuse of illustrations, recitation, broadcasting, reproduction on microfilms or in other ways, and storage in data banks. Duplication of this publication or parts thereof ist only permitted under the provisions of the German Copyright Law of September 9, 1965, in its current version, and a copyright fee must always be paid. Violations fall under the prosecution act of the German Copyright Law.
© Springer-Verlag Berlin Heidelberg 1996 Originally published by Springer-Verlag Berlin Heidelberg New York Tokyo Softcover reprint of the hardcover 1st edition 1996
The use of registered names, trademarks, etc. in this publication does not imply, even in the absence of a specific statement, that such names are exempt from the relevant protective laws and regulations and therefore free for general use.
The publisher cannot assume any legal responsibility for given data, especially as far as directions for the use and the handling of chemicals and biological materials are concerned. This information can be obtained from the instructions on safe laboratory practice and from the manufacturers of chemicals and laboratory equipment.
Production of the plasticfiles: Lux-Piastik oHG, Murnau SPIN: 10076299 51/3020-5 4 3 2 1 0- Printed on acid-free paper
Preface
Recent progress on enzyme immobilisation, enzyme production, coenzyme regeneration and enzyme engineering has opened up fascinating new fields for the potential application of enzymes in a large range of different areas. As more progress in research and application of enzymes has been made the lack of an up-to-date overview of enzyme molecular properties has become more apparent. Therefore, we started the development of an enzyme data information system as part of protein-design activities at GBF. The present book "Enzyme Handbook" represents the printed version of this data bank. In future a computer searchable version will be also available.
The enzymes in this Handbook are arranged according to the Enzyme Commission list of enzymes. Some 3000 "different" enzymes will be covered. Frequently enzymes with very different properties are included under the same EC number. Although we intend to give a representative overview on the characteristics and variability of each enzyme the Handbook is not a compendium. The reader will have to go to the primary literature for more detailed information. Naturally it is not possible to cover all the numerous literature references for each enzyme (for special enzymes up to 40000) if the data representation is to be concise as is intended.
It should be mentioned here that the literature data are extracted from literature and critically evaluated by qualified scientists. On the other hand the original authors' nomenclature for enzyme forms and subunits is retained as is their nomenclature for organisms and strains even if the organism is reclassified in the meantime. The cross references to the protein sequence data bank and to the Brookhaven protein 3D structure data bank are taken directly from their data files without further verification by the authors. In order to keep the tables concise redundant information is avoided as far as possible (e.g. if Km values are measured in the presence of an obvious cosubstrate, only the name of the cosubstrate is given in parentheses as a commentary without reference to its specific role).
The authors are grateful to the following biologists and chemists for invaluable help in the compilation of data: Cornelia Munaretto, Dr. Astrid Beermann, Dr. Ida Schomburg and Astrid Haberz. In addition we would like to thank Mrs. C. Munaretto and Dr. I. Schomburg for the correction of the final manuscript.
Braunschweig, 1996 Dorte Stephan Dietmar Schomburg
v
BRENDA- Compilation of Enzyme Data
To collect basic characteristics of enzymes - is that not a kind of archaic activity in the times of molecular biology and computer-aided data banks providing sequences of nucleic acids and proteins with little more delay than a few days as well as their three-dimensional structures? What should be the purpose of compiling turnover numbers, Michaelis constants, substrate specificities, sources, synonyms etc. of enzymes from sometimes remote publications? The answer sounds as simple as surprising: The aim of the compilation of data is to make use of the overwhelming abundance of structural knoweldge we owe to the new techniques of molecular biology.
Admittedly, it was not primarily enzymology which caused the explosion of knowledge in biology during the last decade. This was due to the advance of molecular biology which enabled us to isolate genes, to amplify them ad libidum and to elucidate their primary structure within days only. Also, the optimization and automatization of techniques for the analysis of macromolecules has provided detailed insights into a large variety of complex biomolecules nobody would have anticipated in the early seventies. Due to powerful computers it has now become feasible to propose fairly realistic models of macromolecules based solely on primary structures and homology considerations.
Nevertheless - or therefore - it appears as mandatory as rewarding to know the brave world of enzymology in which one had and often still has to come along without any detailed structural knowledge. We should not ignore that nature has not generated the multiplicity of structures, because it simply felt obliged to the principle of diversification or because it wanted to test our computing capacity to handle sequence data. It had to create new structures to cope with the steadily changing demands of a variable environment. Thus, amino acid sequences, folding of peptide chains and conformational details are only the technical tools of nature to catalyse specific biological functions. In consequence, it is the functional profile of an enzyme which enables a biologist or physician to analyze a metabolic pathway and its disturbance; it is the substrate specificity of an enzyme which tells an analytical biochemist how to design an assay; it is the stability, specificity and efficiency of an enzyme which determines its usefulness in the biotechnical transformation of a molecule. And the sum of all these functional data will have to be considered when the designer of artificial biocatalysts has to choose the optimum prototype to start with.
Unfortunately, it is by no means as simple to design (organize) a meaningful and systematic compilation of functional enzymological data as to enter sequences of amino acids or nucleotides into a data base. Functional data are less well defined, are never devoid of a trace of ambiguity, their selection remains inevitably subjective, and their complexity requires simplification. The present compilation of enzymological data, therefore, can and will not be a substitute for original publications but rather offer a key to the literature. But I do think that the Enzyme Handbook is indeed an excellent key to open or reopen the mysterious world of
VII
BRENDA- Compilation of Enzyme Data
enzyme to all those who there have to find the solutions of their problems: to biologists, physicians, structural biochemists, biochemical analysts, biotechnologists and also to the molecular biologists.
Braunschweig, Spring 1993 Leopold Flohe GBF, Scientific Director
VIII
List of Abbreviations
A adenosine ER endoplasmic reticulum Ac acetyl Et ethyl ACP acyl-carrier-protein EXAFS extended X-ray absorption ADP adenosine 5'-diphosphate fine structure Ala alanine FAD flavin-adenine dinucleotide All allose FMN flavin mononucleotide (ribo-A it altrose flavin 5'-monophosphate) AMP adenosine 5'-monophosphate FPLC fast protein liquid chroma-Ara arabinose tography Arg arginine Fru fructose Asn asparagine Fuc fucose Asp aspartic acid G guanosine ATP adenosine 5'-triphosphate Gal galactose Bicine N, N'-bis(2-hydroxyethyl) GOP guanosine 5'-diphosphate
glycine Glc glucose c cytidine GleN glucosamine cal calorie GlcNAc N-acetylglucosamine COP cytidine 5'-diphosphate Gin glutamine CDTA trans-1,2-diaminocyclo-hexa- Glu glutamic acid
ne-N, N, N, N-tetra-aceticac id Gly glycine CHAPS 3-[(3-cholamidopropyl)- Glygly glycylglycine
dimethylammonio ]-1- GMP guanosine propanesulfonate 5'-monophosphate
CHAPSO 3-[(3-cholamidopropyl)- GSH glutathione dimethylammonio ]- GSSG oxidized glutathione 2-hydroxy-1-propane- GTP guanosine 5'-triphosphate sulfonate Gul gulose
CMP cytidine 5'-monophosphate h hour Co A coenzyme A H4 tetrahydro CTP cytidine 5'-triphosphate HE PES 4-(2-hydroxyethyl)-1-piper-Cys cysteine azineethane sulfonic acid d deoxy- His histidine D- and L- prefixes indicating HPLC high performance liquid
configuration chromatography DFP diisopropylfluorophosphate Hyl hydroxylysine DNA deoxyribonucleic acid Hyp hydroxyproline DPN diphosphopyridinium IAA iodoacetamide
nucleotide (now NAD) lg immunoglobulin DTNB 5,5'-dithiobis(2-nitrobenzoate) lie isoleucine OTT dithiothreitol (i.e. Cleland's I do idose
reagent) IDP inosine 5'-diphosphate e electron IMP inosine 5'-monophosphate EC number of enzyme in Enzyme ir irreversible
Commission's system ITP inosine 5' -triphosphate E. coli Escherichia coli Km Michaelis constant EDTA ethylene diaminetetraacetate L- seeD-EGTA ethylene glycol bis (~-amino- Leu leucine
ethylether) tetraacetate Lys lysine EPR electron paramagnetic Lyx lyxose
resonance M mol/1
IX
List of Abbreviations
m- meta- rRNA ribosomal RNA Man man nose tRNA transfer RNA MES 2-(N-morpholino )ethane Sar N-methylglycine
sulfonate (sarcosine) Met methionine SDS-PAGE sodium dodecyl sulphate min minute polyacrylamide gel MOPS 3-(N-morpholino) electrophoresis
propane sulfonate Ser serine Mur muramic acid SFK-525A 2-diethylaminoethyl-2,2-MW molecular weight diphenylvalerate NAD nicotinamide-adenine sp. species
dinucleotide T ribosylthymine NADH reduced NAD t1j2 time for half-completion NADP NAD phosphate of reaction NADPH reduced NADP Tal talose NAD(P)H indicates either NADH TOP ribosylthymine
orNADPH 5'-diphosphate NDP nucleoside 5'-diphosphate TEA triethanolamine NEM N-ethylmaleimide TES N-tris[hydroxymethyl]-Neu neuraminic acid methyl-2-amino-NMN nicotinamide ethanesulfonic acid
mononucleotide THF tetrahydrofolate NMP nucleoside Thr threonine
5' -monophosphate TMP ribosylthymine NTP nucleoside 5'-triphosphate 5'-monophosphate 0- ortho- Tos- tosyl-(p-toluenesulfonyl-) OMP orotidine 5-monophosphate TPN triphosphopyridinium Orn ornithine nucleotide (now NADP) p- para-PAPS 3'-phosphoadenylylsulfate Tris tris(hydroxymethyl)-
PCMB p-chloro-mercuribenzoate aminomethane
PEG polyethylene glycol Trp tryptophan
PEP phosphoenolpyruvate TTP ribosylthymine pH -log1o [H+] 5'-triphosphate
Ph phenyl Tyr tyrosine
Phe phenylalanine u uridine PIXE proton-induced U/mg Jlmol/(mg·min)
X-ray emission UDP uridine 5'-diphosphate PMSF phenyl methane- UMP uridine 5'-monophosphate
sulfonylfluoride UTP uridine 5'-triphosphate Pro proline uv ultraviolet 010 factor for the change in Val valine
reaction rate for a 1 oo Xaa symbol for an amino temperature increase acid of unknown consti-
r reversible tution in peptide formula Rha rhamnose XAS X-ray absorption Rib ribose spectroscopy RNA ribonucleic acid XTP xanthosine 5'-triphosphate mRNA messenger RNA Xyl xylose
X
Index (Alphabetical order of Enzyme names)
EC-No. Name
2.2. 1.4 Acetoin-ribose-5-phosphate transaldolase
2.3. 1.9 Acetyi-CoA C-acetyltransferase
2.3. 1.16 Acetyi-CoA C-acyltransferase
2.3. 1.44 N-Acetylneuraminate 4-0-acetyltransferase
2.3. 1.45 N-Acetylneuraminate 7-0 (or 9-0 )-acetyltransferase
2.1. 1.4 Acetylserotonin N-methyltransferase
2.3. 1.38 [Acyl-carrier-protein] 8-acetyltransferase
2.3. 1.39 [Acyl-carrier-protein] 8-malonyltransferase
2.3. 1.40 Acyl-[ acyl-carrier-protein]phospholipid 0-acyltransferase
2.3. 1.129 Acyl-[acyl-carrier-protein]UDP-N-acetylglucosamine 0-acyltransferase
2.3. 1 .22 2-Acylglycerol 0-acyltransferase
2.3. 1.51 1-Acylglycerol-3-phosphate 0-acyltransferase
2.3. 1 .52 2-Acylglycerol-3-phosphate 0-acyltransferase
2.3. 1.23 1-Acylglycerophosphocholine 0-acyltransferase
2.3. 1 .62 2-Acylglycerophosphocholine 0-acyltransferase
2.3. 1 .64 Agmatine N4-coumaroyltransferase
2. 1.2. 7 D-Aianine 2-hydroxymethyl-transferase
2.3. 1.84 Alcohol 0-acetyltransferase 2.3. 1.104 1-Aikenylglycerophospho
choline 0-acyltransferase 2.3. 1.121 1-Aikenylglycerophospho
ethanolamine 0-acyltransferase
2.3. 1.125 1-Aikyl-2-acetylglycerol 0-acyltransferase
EC-No. Name
2.3. 1.105 Alkylglycerophosphate 2-0-acetyltransferase
2.3. 1 .67 1-Aikylglycerophosphocholine 0-acetyltransferase
2.3. 1.63 1-Aikylglycerophosphocholine 0-acyltransferase
2.1. 1.49 Amine N-methyltransferase 2.3. 1.47 8-Amino-7-oxononanoate
synthase 2.3. 1 .36 0-Amino-acid N-acetyltrans
ferase 2.3. 1.1 Amino-acid N-acetyltrans-
ferase 2.3. 1.81 Aminoglycoside N3'-acetyl
transferase 2.3. 1 .82 Aminoglycoside N6'-acetyl-
transferase 2.3. 1 .37 5-Aminolevulinate synthase 2.1 .2. 10 Aminomethyltransferase 2.3. 1.144 Anthranilate N-benzoyl-
transferase 2.3. 1. 113 Anthranilate N-malonyl
transferase 2.1. 1. 111 Anthranilate N-methyltrans
ferase 2.1. 1. 75 Apigenin 4'-0-methyltrans
ferase 2.3. 1 .87 Aralkylamine N-acetyltrans
ferase 2.3. 1.109 Arginine N-succinyltrans
ferase 2.3. 1 .56 Aromatic-hydroxylamine
0-acetyltransferase 2.3. 1 .5 Arylamine N-acetyltrans
ferase 2.3. 1.17 Aspartate N-acetyltrans
ferase 2.1 .3.2 Aspartate carbamoyltrans
ferase 2.1. 1.105 N-Benzoyl-4-hydroxy
anthranilate 4-0-methyltransferase
2.1. 1.92 Bergaptol 0-methyltransferase
XI
EC-No. Name
2.1.1.5 Betaine-homocysteine S-methyltransferase
2.1.1.68 Caffeate 0-methyltransferase
2.1.1.1 04 Caffeoyi-CoA a-methyltransferase
2.1.1.60 Calmodulin-lysine N-methyltransferase
2.3.1. 7 Carnitine 0-acetyltransferase
2.3.1.137 Carnitine 0-octanoyltransferase
2.3.1.21 Carnitine 0-palmitoyltransferase
2.1.1.22 Carnosine N-methyltransferase
2.1.1.6 Catechol 0-methyltransferase
2.3.1. 70 CDPacylglycerol 0-arach idonyltransferase
2.3.1.28 Chloramphenicol a-acetyltransferase
2.3.1.98 Chlorogenate-glucarate 0-hydroxycinnamoyltransferase
2.3.1.6 2.3.1.27 2.1.1.79
Choline 0-acetyltransferase Cortisol 0-acetyltransferase Cyclopropane-fatty-
acyl phospholipid synthase
2.3.1.80 Cysteine-S-conjugate N-acetyltransferase
2.1.1.59 Cytochrome-c-lysine N-methyltransferase
2.3.1.49 Deacetyl-[citrate-(pro-38)lyase] S-acetyltransferase
2.3.1.1 07 17-0-Deacetylvindoline 0-acetyltransferase
2.1.1.94 11-0-Demethyi-17-Qdeacetylvindoline 0-methyltransferase
2.1.1.102 Demethylmacrocin 0-methyltransferase
2.1.1.38 0-Demethylpuromycin 0-methyltransferase
2.1.1.1 09 Demethylsterigmatocystin 6-0-methyltransferase
XII
EC-No. Name
2.1.1.64 3-Demethylubiquinone-9 3-0-methyltransferase
2.1.2.8 Deoxycytidylate 5-hydroxymethyltransferase
2.1.1.54 Deoxycytidylate C-methyltransferase
2.3.1.20 Diacylglycerol 0-acyltransferase
2.3.1.73 Diacylglycerol-sterol 0-acyltransferase
2.3.1.57 Diamine N-acetyltransferase
2.3.1.58 2,3-Diaminopropionate N-oxalyltransferase
2.3.1.114 3,4-Dichloroaniline N-malonyltransferase
2.3.1.12 Dihydrolipoamide acetyltransferase
2.3.1.61 Dihydrolipoamide S-succinyltransferase
2.1.1.44 Dimethylhistidine N-methyltransferase
2.1.1.83 3, 7-Dimethylquercitin 4 '-o-methyltransferase
2.1.1.98 Diphthine synthase 2.1.1.37 DNA (cytosine-5-)-methyl
transferase 2.3.1.123 Dolichol 0-acyltransferase 2.3.1.139 Ecdysone 0-acyltrans
ferase 2.3.1.94 Erythronolide synthase 2.1.1.15 Fatty-acid 0-methyltrans-
ferase 2.3.1.85 Fatty-acid synthase 2.3.1.86 Fatty-acyi-CoA synthase 2.3.1.116 Flavonol-3-0-beta-
glucoside a-malonyltransferase
2.2.1.3 Formaldehyde trans keto lase
2.3.1.54 Formate C-acetyltransferase
2.3.1.101 Formylmethanofurantetrahydromethanopterin N-formyltransferase
2.3.1.130 Galactarate 0-hydroxycinnamoyltransferase
EC-No. Name
2.3.1.134 Galactolipid a-acyltransferase
2.31.18 Galactoside a-acetyltransferase
2.3.1.141 Galactosylacylglycerol a-acyltransferase
2.3.1.59 Gentamicin 2'-N-acetyltransferase
2.3.1.60 Gentamicin 3'-N-acetyltransferase
2.3.1.131 Glucarate a-hydroxycinnamoyltransferase
2.3.1.132 Glucarolactone a-hydroxycin namoyltransferase
2.3.1.90 beta-Giucogallin a-galloyltransferase
2.3.1.143 beta-Giucogallintetrakisgalloylglucose
2.3.1.3 Glucosamine N-acetyltransferase
2.3.1.4 Glucosamine-phosphate N-acetyltransferase
2.1.1.112 Glucuronoxylan 4-a-methyltransferase
2.3.1.35 Glutamate N-acetyltransferase
2.1.2.5 Glutamate formiminotrans-
2.3.1.68
2.3.1.14
2.3.1.15
2.3.1.42
2.3.1.29 2.3.1.13 2.1.4.1 2.3.1.71
2.3.1.65
2.1.2.4
2.1.2.1
ferase Glutamine N-acyltrans
ferase Glutamine N-phenylacetyl
transferase Glycerol-3-phosphate
a-acyltransferase Glycerone-phosphate
a-acyltransferase Glycine C-acetyltransferase Glycine N-acyltransferase Glycine amidinotransferase Glycine N-benzoyltrans-
ferase Glycine N-choloyltrans
ferase Glycine formiminotrans
ferase Glycine hydroxymethyl
transferase
EC-No. Name
2.1.1.20 Glycine N-methyltransferase
2.3.1.142 Glycoprotein a-fatty-acyltransferase
2.3.1.96 Glycoprotein N-palmitoyltransferase
2.3.1.97 Glycylpeptide N-tetradecanoyltransferase
2.1.1.2 Guanidinoacetate N-methyltransferase
2.3.1.78 Heparan-alpha-glucos aminide N-acetyltransferase
2.1.1.8 Histamine N-methyltransferase
2.3.1.33 Histidine N-acetyltransferase
2.3.1.48 Histone acetyltransferase 2.1.1.43 Histone-lysine N-methyl
transferase 2.1.1.10 Homocysteine S-methyl
transferase 2.3.1.31 Homoserine a-acetyltrans
ferase 2.3.1.46 Homoserine a-succinyl
transferase 2.3.1.10 Hydrogen-sulfideS-acetyl
transferase 2.1.1.97 3-Hydroxyanthranilate
4-C-methyltransferase 2.3.1.118 N-Hydroxyarylamine
a-acetyltransferase 2.1.1.69 5-Hydroxyfuranocoumarin
5-a-methyltransferase 2.1.1. 70 8-Hydroxyfuranocoumarin
8-a-methyltransferase 2.3.1.93 13-Hydroxylupanine
a-tigloyltransferase 2.3.1.102 N6-Hydroxylysine a-acetyl
transferase 2.1.1.108 6-Hydroxymellein a-methyl
transferase 2.1.3. 7 3-Hydroxymethylcephem
carbamoyltransferase 2.1.1.88 8-Hydroxyquercitin
8-a-methyltransferase 2.3.1.119 lcosanoyi-CoA synthase
XIII
EC-No. Name EC-No. Name
2.3.1.2 Imidazole 2.1.1.12 Methionine 8-methyl-N-acetyltransferase transferase
2.3.1.72 lndoleacetylglucose- 2.1.2.9 Methionyl-tRNA inositol 0-acyltransferase formyltransferase
2.1.1.47 lndolepyruvate C-methyl- 2.1.1.99 16-Methoxy-2,3-dihydro-3-transferase hyd roxytaberson i ne
2.1.4.2 lnosamine-phosphate N-methyltransferase amidinotransferase 2.1.2.11 3-Methyl-2-oxobutanoate
2.1.1.39 myo-lnositol 1-0-methyl- hydroxymethyltransferase transferase 2.1.1.21 Methylam i ne-g I utamate
2.1.1.40 myo-lnositol 3-0-methyl- N-methyltransferase transferase 2.1.1.63 Methylated-DNA-protein-
2.1.1.26 lodophenol 0-methyl- cysteine 8-methyl-transferase transferase
2.1.1.91 lsobutyraldoxime 0-methyl- 2.1.1.16 Methylene-fatty-acyl-transferase phospholipid synthase
2.3.1.126 lsocitrate 0-dihydroxycin- 2.1.1.74 Methylenetetrahydrofolate-namoyltransferase tRNA (uracil-5-)-methyl-
2.3.1.115 lsoflavone-7-0-beta- transferase glucoside 6"-0-malonyl- (FADH2-oxidizing) transferase 2.1.3.1 Methylmalonyi-CoA
2.1.1.46 lsoflavone 4'-0-methyl- carboxyltransferase transferase 2.1.1.84 Methylquercetagetin
2.1.1. 78 lsoorientin 3'-0-methyl- 6-0-methyltransferase transferase 2.1.1.82 3-Methylquercitin
2.3.1.55 Kanamycin 6'-N-acetyl- 7 -0-methyltransferase transferase 2.1.1.13 5-Methyltetrahydrofolate-
2.3.1.66 Leucine N-acetyltransferase homocysteine 2.1.1.65 Licodione 2'-0-methyl- 8-methyltransferase
transferase 2.1.1.14 5-Methyltetrahydropteroyl-2.1.1.50 Loganate 0-methyl- triglutamate-homocysteine
transferase 8-methyltransferase 2.3.1.75 Long-chain-alcohol 2.3.1.69 Monoterpenol
0-fatty-acyltransferse 0-acetyltransferase 2.1.1.42 Luteolin 0-methyl- 2.1.1.56 mRNA (guanine-N 7-)-
transferase methyltransferase 2.3.1.32 Lysine N-acetyltransferase 2.1.1.62 mRNA (2'-0-methyladeno-2.1.3.8 Lysine carbamoyl- sine-N6-)-methyltransferase
transferase 2.1.1.57 mRNA (nucleoside-2'-0-)-2.1.1.101 Macrocin 0-methyl- methyltransferase
transferase 2.3.1.111 Mycocerosate synthase 2.1.1.11 Magnesium protoporphyrin 2.3.1.1 00 Myelin-proteolipid
0-methyltransferase 0-palmitoyltransferase 2.3.1.79 Maltose 0-acetyltransferase 2.3.1.74 Naringenin-chalcone 2.1.1.90 Methanol-5-hydroxybenz- synthase
imidazolylcobamide 2.1.1.1 Nicotinamide Co-methyltransferase N-methyltransferase
XIV
EC-No. Name
2.1. 1. 7 Nicotinate N-methyltransferase
2.3. 1.127 Ornithine N-benzoyltransferase
2.1 .3.3 Ornithine carbamoyl-transferase
2.1 .3.5 Oxamate carbamoyl-transferase
2.3. 1.41 3-0xoacyl-[acyl-carrierprotein] synthase
2.3. 1 .88 Peptide alpha-Nacetyltransferase
2.1. 1 .25 Phenol 0-methyltransferase 2.3. 1.53 Phenylalanine N-acetyl
transferase 2.1. 1 .28 Phenylethanolamine
N-methyltransferase 2.3. 1 .8 Phosphate acetyl-
transferase 2.3. 1.19 Phosphate butyryl
transferase 2.3. 1 .83 Phosphatidylcholine-
dol ichol 0-acyltransferase 2.3. 1.135 Phosphatidylcholine-
retinol 0-acyltransferase 2.3. 1.43 Phosphatidylcholine-
sterol 0-acyltransferase 2. 1. 1.17 Phosphatidylethanolamine
N-methyltransferase 2. 1.1. 71 PhosphatidyiN-methyl
ethanolamine N-methyltransferase
2.1. 1.103 Phosphoethanolamine N-methyltransferase
2.1 .2.3 Phosphoribosylaminoimi-dazolecarboxamide formyltransferase
2.1 .2.2 Phosphoribosylglycinamide formyltransferase
2.3. 1.146 Pinosylvin synthase 2.3. 1.145 Piperidine N-piperoyl
transferase 2.3. 1.25 Plasmalogen synthase 2.1. 1.18 Polysaccharide
0-methyltransferase 2.3. 1.136 Polysialic-ar:ld
0-acetyltransferase
EC-No. Name
2.1. 1.23 Protein-arginine N-methyltransferase
2.1. 1 .80 Protein-glutamate 0-methyltransferase
2.1. 1 .85 Protein-histidine N-methyltransferase
2.1. 1. 77 Protein-L-isoaspartate( 0-aspartate) 0-methyltransferase
2.1. 1.100 Protein-S-isoprenylcysteine 0-methyltransferase
2.1 .3.6 Putrescine carbamoyl-transferase
2.3. 1.138 Putrescine N-hydroxycinnamoyltransferase
2.1. 1 .53 Putrescine N-methyltransferase
2.1. 1 .87 Pyridine N-methyltransferase 2. 1.1. 76 Quercetin 3-0-methyl
transferase 2.3. 1 .99 Quinate 0-hydroxycinna
moyltransferase 2.3. 1.76 Retinol 0-fatty-acyl
transferase 2.3. 1.128 Ribosomal-protein-alanine
N-acetyltransferase 2.3. 1.140 Rosmarinate synthase 2.1 1.48 rRNA (adenine-N6-)-methyl
transferase 2.1. 1 .66 rRNA (adenosine-2'-0-)
methyltransferase 2.1. 1.51 rRNA (guanine-NL)-methyl
transferase 2.1. 1.52 rRNA (guanine-N2-)-methyl-
transferase 2.3. 1 .30 Serine 0-acetyltransferase 2.31 .50 Serine C-palmitoyltransferase 2.3. 1 133 Shikimate 0-hydroxycin-
namoyltransferase 2.3. 1.91 Sinapoylgiucose-choline
0-sinapoyltransferase 2.3 1.92 Sinapoylglucose-malate
0-sinapoyltransferase 2.3.1 103 Sinapoylglucose
sinapoylglucose Osinapnyltransferase
XV
EC-No. Name
2.1.1. 72 Site-specific DNA-methyltransferase (adenine-specific)
2.1.1. 73 Site-specific DNA-methyltransferase (cytosine-specific)
2.1.1.113 Site-specific· DNA-methyltransferase ( cytosine-N 4-specific)
2.3.1.24 Sphingosine N-acyltransferase
2.1.1.11 0 Sterigmatocystin 7 -0-methyltransferase
2.3.1.26 Sterol 0-acyltransferase 2.1.1.41 24-Sterol C-methyl
transferase 2.3.1.106 Tartronate 0-hydroxycin
namoyltransferase 2.1.1.89 Tetrahydrocolumbamine
2-0-methyltransferase 2.3.1.89 Tetrahydrodipicolinate
N-acetyltransferase 2.1.1.86 Tetrahydromethan
opterin 8-methyltransferase
2.3.1.117 2,3,4,5-Tetrahydropyridine-2-carboxylate N-succinyltransferase
2.1.1.3 Thetin-homocysteine 8-methyltransferase
2.3.1.11 Thioethanolamine S-acetyltransferase
2.1.1.96 Thioether S-methyltransferase
2.1.1.9 Thiol S-methyltransferase 2.1.1.67 Thiopurine S-methyl
transferase 2.1.1.45 Thymidylate synthase 2.1.1.95 Tocopherol a-methyl
transferase 2.2.1.2 Transaldolase 2.2.1.1 Transketolase
XVI
EC-No. Name
2.3.1.122 Trehalose 0-mycolyltransferase
2.3.1.77 Triacylglycerol-sterol 0-acyltransferase
2.3.1.95 Trihydroxystilbene synthase 2.1.1.19 Trimethylsulfonium
tetrahydrofolate N-methyltransferase
2.1.1.36 tRNA (adenine-N 1-)-
methyltransferase 2.1.1.55 tRNA (adenine-N6-)
methyltransferase 2.1.1.29 tRNA (cytosine-5-)
methyltransferase 2.1.1.31 tRNA (guanine-NL)
methyltransferase 2.1.1.32 tRNA (guanine-N2._)
methyltransferase 2.1.1.33 tRNA (guanine-N7-)
methyltransferase 2.1.1.34 tRNA (guanosine-2'-0-)
methyltransferase 2.1.1.61 tRNA (5-methylamino
methyl-2-thiouridylate )methyltransferase
2.1.1.35 tRNA (uracil-5-)methyltransferase
2.3.1.34 D-Tryptophan N-acetyltransferase
2.3.1.112 D-Tryptophan N-malonyltransferase
2.1.1.1 06 Tryptophan 2-C-methyltransferase
2.3.1.108 Tubulin N-acetyltransferase 2.3.1.11 0 Tyramine N-feruloyl
transferase 2.1.1.27 Tyramine N-methyl
transferase 2.1.1.1 07 Uroporphyrin-Ill
C-methyltransferase 2.1.1.93 Xanthotoxol
0-methyltransferase