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D. Schamburg · D. Stephan (Eds.)
GBF- Gesellschaft für Biotechnologische Forschung
Enzyme Handbock
8
Class 1.13-1.97: Oxidoreductases
Springer-Verlag Berlin Haideiberg GmbH
Professor Dr. Dietmar Schomburg
Dr. Dörte Stephan
GBF - Gesellschaft für Biotechnologische Forschung mbH
Mascheroder Weg 1
38124 Braunschweig
FRG
This collection of datasheets was generated from the database .. BRENDA •
ISBN 978-3-642-47751-5
Library of Congress Cataloging-in-Publication Data. (Revised for volume 8). Enzyme hand
book. Vols. 6-7 edited by D. Schornburg, M. Salzmann. D. Stephan. Loose-leaft. lncludes
bibliographical references and indexes. Contents: v. 1.C lass 4: Lyases-v. 2. Class 5: lso
merases. - etc. - v. 8.C lass 1.13--1.97, Oxidoreductases. 1. Enzymes-Handbooks, ma
nuals. etc. I. Schornburg, D.( Dietmar) II. Salzmann, M. (Margit) I. Stephan, D. (DOrte)
OP601.E5158 1990 560'.634 91-145566
ISBN 978-3-642-47751-5 ISBN 978-3-642-57942-4 (eBook)
001 10.1007/978-3-642-57942-4
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~Springer-Verlag Berlin Heidelberg 1994
Originally published by Springer-Verlag Berlin Haideiberg New York in 1994
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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
Iack of an up-to-date overview of enzyme molecular properties has become
more apparent. Therefore, we started the development of an enzyme data in
formation system as part of protein-design activities at GBF. The present
book "Enzyme Handbook" represents the printed version of this data bank. ln
future a computer searchable versionwill be also available.
The enzymes in this Handbock are arranged according to the Enzyme
Commission Iist 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 Handbock is not a com
pendium. The readerwill have to go to the primary Iiterature for more detailed
information. Naturally it is not possible to cover all the numerous Iiterature
references for each enzyme (for special enzymes up to 40000) if the data re
presentation is tobe concise as is intended.
lt should be mentioned here that the Iiterature data are extracted from
Iiterature 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 reclas
sified in the meantime. The crass references to the protein sequence data
bank and to the Brookhaven protein 30 structure data bank are taken direct
ly from their data files without further verification by the authors. ln order to
keep the tables concise redundant information is avoided as far as possible
(e.g. if Km values are measured in the presence af an obviaus cosubstrate, on
ly 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 invalu
able help in the compilatian af data: Margit Salzmann, Cornelia Munaretto,
Dr. lda Schamburg, Dr. Astrid Beermann. ln addition we wauld like ta thank
Mrs. C. Munaretto and Dr. I. Schamburg for the correctian af the final manu
script.
Braunschweig, Spring 1994 Dörte Stephan
Dietmar Schamburg
V
BRENDA-Compilation of Enzyme Data
To collect basic characteristics of enzymes- is that not a kind of archaic ac
tivity 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 weil as their three-dimensional structures? What should be the
purpese of compiling turnever 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 struc
tural 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 op
timization and automatization of techniques for the analysis of macro
molecules 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 propese 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
feit obliged to the principle of diversification or because it wanted to test our
computing capacity to handle sequence data. lt 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.
ln 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 substrafe specificity of an enzyme which teils an analytica/ bioehernist
how to design an assay; it is the stability, specificity and efficiency of an en
zyme which determines its usefulness in the biotechnica/ 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 meaning
ful and systematic compilation of functional enzymological data as to enter
sequences of amino acids or nucleotides into a data base. Functional data
are less weil 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
VII
BRENDA-Compilation of Enzyme Data
Substitute for original publications but rather offer a key to the literature. But I
do think that the Enzyme Handbock is indeed an excellent key to open or
reopen the mysterious world of 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 DPN diphosphopyridinium
Ac acetyl nucleotide (now NAD)
ADP adenosine 5'- DTNB 5,5'-dithiobis
diphosphate (2-nitrobenzoate)
Ala alanine DTT dithiothreitol
All allose (i.e. Cleland's reagent)
Alt altrase e electron
AMP adenosine 5'- EC number of enzymein
monophosphate Enzyme Commission's
Ara arabinose system
Arg arginine E.coli Escherichia coli
Asn asparagine EDTA ethylene
Asp aspartic acid diaminetetraacetate
ATP adenosine 5'- EGTA ethylene glycol bis
triphosphate (ß-aminoethyl ether)
Bicine N,N'-bis(2-hydroxyethyl) tetraacetate
glycine EPR electron paramagnetic
c cytidine resonance
cal calorie ER endoplasmic reticulum
COP cytidine 5'-diphosphate Et ethyl
CDTA trans-1,2- EXAFS extended X-ray
diaminocyclohexane- absorption fine
N, N. N,N-tetra-acetic structure
acid FAD flavin-adenine
CHAPS 3-[(3-cholamidopropyl)- dinucleotide
dimethylammonio]-1- FMN flavin mononucleotide
propanesulfonate (riboflavin 5'-
CHAPSO 3-[(3-cholamidopropyl)- monophosphate)
dimethylammonio]-2- Fru fructose
hydroxy-1-propane- Fuc fucose
sulfonate G guanosine
CMP cytidine 5'- Ga I galactose
monophosphate GDP guanosine 5'-
CoA coenzymeA diphosphate
CTP cytidine 5'-triphosphate Glc glucose
Cys cysteine GieN glucosamine
d deoxy- GlcNAc N-acetylglucosamine
0-and L- prefixes indicating con- Gin glutamine
figuration Glu glutamic acid
DFP diisopropyl Gly glycine
fluorophosphate GMP guanosine 5'-
DNA deoxyribonucleic acid monophosphate
IX
List of Abbreviations
GSH glutathione NAD(P)H indicates either NADH
GSSG oxidized glutathione orNADPH
GTP guanosine 5'- NDP nucleoside
triphosphate 5'-diphosphate
Gul gulose NEM N-ethylmaleimide
h hour Neu Neuraminic acid
H4 tetrahydro NMN nicotinamide
HE PES 4-(2-hydroxyethyl)- mononucleotide
1-piperazineethane NMP nucleoside
sulfonic acid 5' -monophosphate
His histidine NTP nucleoside
HPLC highperformanceliquid 5' -triphosphate
chromatography 0- ortho-
Hyl hydroxylysine Orn ornithine
Hyp hydroxyproline p- para-
IAA iodoacetamide PCMB p-chloro-
lg immunoglobulin mercuribenzoate
lle isoleueine PEP phosphoenolpyruvate
ldo idose pH -log10 [H+]
IDP inosine 5'-diphosphate Ph phenyl
IMP inosine Phe phenylalanine
5' -monophosphate PI XE proton-induced
ir irreversible X-ray emission
ITP inosine 5'-triphosphate PMSF phenylmethane-
Km Michaelis constant su lfo nylfl uoride
L- see D- Pro proline
Leu leueine O,o factor for the change in
Lys Iysine reaction rate for a 10 o
Lyx lyxose temperature increase
M mol/1 r reversible
m- meta- Rha rhamnose
Man mannose Rib ribose
MES 2-(N-morphol ino )ethane RNA ribonucleic acid
sulfonate mRNA messenger RNA
Met methionine rRNA ribosemal RNA
min minute tRNA transfer RNA
MOPS 3-(N-morpholino) Sar N-methylglycine
propane sulfonate (sarcosine)
Mur muramic acid SOS-PAGE sodium dodecyl sul-
MW molecular weight phate polyacrylamide
NAD nicotinamide-adenine gel electrophoresis
dinucleotide Ser serine
NADH reduced NAD SFK-525A 2-diethylaminoethyl-2,2-
NADP NAD phosphate diphenylvalerate
NADPH reduced NADP sp. species
X
List of Abbreviations
T ribosylthymine TTP ribosylthymine
ty, time for half-completion 5' -triphosphate
of reaction Tyr tyrosine
Tal talose u uridine
TOP ribosylthymine U/mg Jlmol/(mg·min)
5'-diphosphate UDP uridine 5'-diphosphate
TEA triethanolamine UMP uridine
THF tetrahydrofolate 5' -monophosphate
Thr threonine UTP uridine 5'-triphosphate
TMP ribosylthymine Val valine
5' -monophosphate Xaa symbol for an amino
Tos- tosyl- acid of unknown
(p-toluenesulfonyl-) constitution in peptide
TPN triphosphopyridinium formula
nucleotide XAS X-ray absorption
(now NADP) spectroscopy
Tris tris(hydroxymethyl)- XTP xanthosine
aminomethane 5' -triphosphate
Trp tryptophan Xyl xylose
XI
