Table Of ContentD. Schomburg · M. Salzmann (Eds.)
GBF- Gesellschaft fUr Biotechnologische Forschung
Enzyme Handbook
1
Class 4: Lyases
Springer-Verlag Berlin Heidelberg GmbH
Professor Dr. Dietmar Schomburg
Margit Salzmann
GBF-Gesellschaft fUr Biotechnologische Forschung mbH
Marscheroder Weg 1
D-3300 Braunschweig, FRG
This collection of datasheets was generated from the database ,BRENDA"
ISBN 978-3-642-49127-6 ISBN 978-3-642-86605-0 (eBook)
DOI 10.1007/978-3-642-86605-0
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© Springer-Verlag Berlin Heidelberg 1990
Originally published by Springer-Verlag Berlin Heidelberg New York Tokyo in 1990
Softcover reprint of the hardcover 1st edition 1990
The use of registered names, trademarks, etc. in this publication does not imply, even in the
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The publisher cannot assume any legal responsibility for given data, especially as far as
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This information can be obtained from the instructions on safe laboratory practice and from
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Preface
Recent progress in 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
more apparent has become the lack of an up-to-date overview of enzyme
molecular properties. The need for such a data bank was also expressed by
the EC-task force "Biotechnology and Information". 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 it is also planned to make a com
puter searchable version available.
The enzymes in the Handbook are arranged according to the 1984 Enzyme
Commission list of enzymes and later supplements. Some 3000 "different" en
zymes are covered. Frequently very different enzymes are included under the
same E. C. number. Although we intended to give a representative overview
on the molecular variability of each enzyme, the Handbook is not a com
pendium. The reader will have to go to the primary literature for more detailed
information. Naturally it is not possible to cover all numerous, up to 40 000,
literature references for each enzyme if data representation is to be concise
as is intended.
The authors are grateful to the following bioligists and chemists for invalu
able help in the compilation of data, expecially Cornelia Munaretto, Dr. Ida
Schomburg, Dr. Sabine Vogei-Ziebolz, Uwe Hirschganger, lnka Siegmund and
Roland Vogt. Mrs. C. Munaretto and Dr. I. Schomburg are also thanked for
the correction of the final manuscript.
Braunschweig Margit Salzmann
June, 1990 Dietmar Schomburg
v
BRENDA-Enzyme Data for Research and Production
Enzymes are used in all parts of the living world for catalysis of innumerable
biochemical reactions. It has been known for some time that they represent
potentially highly interesting catalysts for chemical research and production
because of their high efficiency, stereospecifity, and their regio- and
enantioselectivity. Enormous progress has been made in recent years in en
zyme immobilisation, stabilisation, coenzyme regeneration etc., while gene
technology has made possible the production of large quantities of otherwise
inaccessible enzymes. Enzyme-design methods and recent work on enzyme
behaviour in organic solvents have opened further possibilities for their use in
new application areas. In addition to the chemical industry their use in the
food industry and environmental technology is worthy of mention.
A number of problems still have to be overcome before enzymes take their
place besides the other commonly used catalysts in the chemical laboratory,
productions and in the awareness of the chemist and the general public. So
the current industrial use of enzymes is more or less limited to proteases and
carbohydrases, i. e. hydrolytic enzymes. Other synthetically important reac
tions such as the forming of C-C bonds are rarely achieved enzymatically at
present. In addition to the real problems (price, too high selectivity etc.) reser
vations on the part of the chemists prohibit decisions about their potential
use.
This is mainly caused by the undeniable fact that information about en
zymes is not as easily obtained as that about other synthetic means and
catalysts. Results of enzyme research are often published in journals which
are rarely read by most chemists and are often not available in organic
chemistry libraries. The published data on molecular weight, stability etc. can
be contradictory, the use of a number of different names for the same en
zyme is common, and the systematic classification of the enzyme is usually
unsatisfactory.
The apparently simple question:
"Is there an enzyme, that catalyzes the enantioselective replacement of an
hydrogen atom in an a-position to an aromatic ring and is stable in a water
solution with a certain pH-value and a given temperature?"
can often only be answered after intensive work in a library or the use litera
ture data bases. A rational choice between several potential enzyme
catalyzed reaction paths is imposible in a reasonable time. When planning
research projects in the area of enzyme design, information about potential
enzymes and use of the correct initial enzyme is also essential.
In addition to the above types of chemical problem, systematic biochemical
investigations are central to the wide interest in enzymes, therefore a great
deal of information can be gained from establishment of a comprehensive
collection of enzyme data.
VII
BRENDA-Enzyme Data for Research and Production
In the GBF research programme, enzyme technology has always played a
significant role. This is documented by innovative contributions in the field of
cofactor regeneration, enzyme production by genetic engineering and down
stream processing after fermentation.
The area has gained new significance from the activities in protein design
where the central theme is protein structure determination and biocomputing.
It soon became evident that the next logical step was the development of
an enzyme data bank which could be undertaken by the group for molecular
structure research. We hope that publication of this comprehensive, critical
literature evaluation will be of wide interest to external users and, in this way,
we hope the GBF has provided a further important contribution to the in
formation infrastructure in biotechnology.
Braunschweig Joachim Klein
June, 1990 GBF, Scientific Director
VIII
List of Abbreviations
Ac acetyl EGTA ethylene glycol bis
AOP adenosine 5'- (P-aminoethyl ether)
diphosphate tetraacetate
Ala alanine ER endoplasmic reticulum
All allose Et ethyl
A It altrose FAD flavin-adenine
AMP adenosine 5'- dinucleotide
monophosphate FMN flavin mononucleotide
Ara arabinose (riboflavin 5'-
Arg arginine monophosphate)
Asn asparagine Fru fructose
Asp aspartic acid Fuc fucose
ATP adenosine 5'- Gal galactose
triphosphate GOP guanosine 5'-
cal calories diphosphate
COP cytidine 5'-diphosphate Glc glucose
COTA trans-1 ,2- GleN glucosamine
diaminocyclohexane- GlcNAc N-acetylglucosamine
N, N, N, N-tetra -acetic Gin glutamine
acid Glu glutamic acid
CMP cytidine 5'- Gly glycine
monophosphate GMP guanosine 5'-
Co A coenzyme A monophosphate
CTP cytidine 5'-triphosphate GTP guanosine 5'-
Cys cysteine triphosphate
d deoxy- Gul gulose
D- H4 tetra hydro
and L- prefixes indicating con- His histidine
figuration HPLC high pressure liquid
DFP diisopropyl chromatography
fluorophosphate IAA iodoacetamide
DNA deoxyribonucleic acid lg immunoglobulin
OPN diphosphopyridinium lie isoleucine
nucleotide (now NAD) Id o idose
DTNB 5,5'-dithiobis (2- lOP inosine 5' -diphosphate
nitro benzoate) IMP inosine
EC number of enzyme in 5'-monophosphate
Enzyme Commis- ITP inosine 5'-triphosphate
sian's system Km concentration of
E. coli Escherichia coli substrate giving half
EDTA ethylene maximum velocity
d iami netetraacetate (Michaelis constant)
IX
List of Abbreviations
L- seeD- PCMB p-chloro-
Leu leucine mercuribenzoate
Lys lysine PEP phosphoenolpyruvate
Lyx lyxose pH -log10 [H]
M gm molecule (1 mole) Ph phenyl
per litre Phe phenylalanine
m- meta- PMSF phenylmethane-
Man man nose sulfonylfluoride
MES 2-(N-morpholino )ethane Pro proline
sulfonate 010 temperature coefficient
Met methionine for a reaction
mM 10-3Mole Rha rhamnose
Mur muramic acid Rib ribose
MW molecular weight RNA ribonucleic acid
NAD nicotinamide-adenine mRNA messenger RNA
dinucleotide (state of rRNA ribosomal RNA
oxidation tRNA transfer RNA
unspecified) SDS- sodium dodecyl sui-
NAD+ nicotinamide-adenine PAGE ph ate
dinucleotide (oxidized (=sodium lauryl sui-
form) phate)-
NADH reduced NAD polyacrylamide
NADP NAD phosphate gel electrophoresis
(state of oxidation Ser serine
unspecified) t,, time for half-completion
NADP+ NADP (oxidized form) of reaction
NAD(P)+ indicates either NAD + Tal talose
orNADP+ TOP ribosylthymine
NADPH reduced NADP 5'-diphosphate
NAD(P)H indicates either NADH Thr threonine
orNADPH TMP ri bosylthym i ne
NDP nucleoside 5'-monophosphate
5'-diphosphate Tos- tosyl-
NEM N-ethylmaleimide (p-toluenesulfonyl-)
Neu Neuraminic acid TPN trip hosphopyrid in i u m
o-
nm nanometre (1 9 metre) nucleotide
NMN nicotinamide (nowNADP)
mononucleotide Tris tris(hydroxymethyl)-
NMP nucleoside aminomethane
5'-monophosphate Trp tryptophan
NTP nucleoside TTP ribosylthymine
5' -triphosphate 5'-triphosphate
0- ortho- Tyr tyrosine
Orn ornithine U/mg J.lmol/(mg*min)
p- para- UDP uridine 5'-diphosphate
X
List of Abbreviations
UMP uridine Xaa symbol for an amino
5'-monophosphate acid of unknown con
UTP uridine 5' -triphosphate stitution in peptide
Val valine formula
Xyl xylose
XI
