10.1006 abbi.1998.0845.csv

Substrates ['DL-threo-beta-phenylserine', 'NAD+'],Products ['DL-2-amino-3-phenyl-3-oxopropionate', 'NADH']
Aronson,0
R.L.,0
Su,0
M.R.,0
Biol.,0
106,0
1976,0
27,0
59,0
6,0
P.A.,0
Craig,0
E.E.,0
Dekker,0
Biochemistry,0
25,0
1986,0
1870,0
1876,0
7,0
P.A.,0
Craig,0
E.E.,0
Dekker,0
Biochim.,0
Biophys.,0
Acta,0
957,0
1988,0
222,0
229,0
8,0
P.A.,0
Craig,0
E.E.,0
Dekker,0
Biochim.,0
Biophys.,0
Acta,0
1037,0
1990,0
30,0
38,0
9,0
A.R.,0
Johnson,0
E.E.,0
Dekker,0
Protein,0
Sci.,0
5,0
1996,0
382,0
390,0
10,0
Y.-W.,0
Piperno,0
D.L.,0
Oxender,0
J.,0
Biol.,0
Chem.,0
243,0
1968,0
5914,0
5920,0
29,0
J.P.,0
Regular,0
Article,0
Investigation,0
of,0
a,0
Catalytic,0
Zinc,0
Binding,0
Site,0
inEscherichia,0
coli,2
l-Threonine,0
Dehydrogenase,0
by,0
Site-Directed,0
Mutagenesis,0
of,0
Cysteine-38,0
Adam,0
R.,0
Johnson,0
2,0
Yen-Wen,0
Chen,0
3,0
Eugene,0
E.,0
Dekker,0
4,0
Department,0
of,0
Biological,0
Chemistry,0
University,0
of,0
Michigan,0
Ann,0
Arbor,0
Michigan,0
48109,0
2,0
Current,0
address:,0
Department,0
of,0
Biochemistry,0
Parke-Davis,0
Pharmaceutical,0
Research,0
Division,0
Warner-Lambert,0
Co.,0
Ann,0
Arbor,0
MI,0
48105.,0
Somerville,0
B.R.,0
Without,0
added,0
Zn2+,0
mutant,0
C38D,0
is,0
equally,0
active,0
with,0
threonine,0
and,0
2-amino-3-hydroxypentanoate,0
but,0
Zn2+-activated,0
mutant,0
C38D,0
is,0
10-fold,0
more,0
reactive,0
with,0
threonine,0
than,0
with,0
2-amino-3-hydroxypentanoate.,0
Chen,0
E.E.,0
Dekker,0
J.E.,0
Biochem.,0
Biophys.,0
316,0
1995,0
413,0
420,0
28,0
J.R.,0
Ganzhorn,0
B.V.,0
Plapp,0
J.,0
Biol.,0
Chem.,0
263,0
1988,0
5446,0
5454,0
31,0
E.,0
Magonet,0
P.,0
Hayen,0
D.,0
Delforge,0
E.,0
Delaive,0
J.,0
Remacle,0
Biochem.,0
J.,0
Pringle,0
M.,0
Osborn,0
Methods,0
Enzymol.,0
26,0
1972,0
3,0
27,0
27,0
J.P.,0
Gibson,0
G.F.,0
Mutants,0
C38S,0
and,0
C38D,0
were,0
purified,0
to,0
homogeneity,0
and,0
found,0
to,0
be,0
like,0
the,0
wild-type,0
enzyme,0
homotetrameric,0
proteins,0
containing,0
one,0
Zn2+atom,0
per,0
subunit.,0
Penner-Hahn,0
Inorg.,0
Chim.,0
Acta,0
275–276,0
1998,0
215,0
221,0
5,0
H.,0
Eklund,0
B.,0
Nordström,0
E.,0
Zeppezauer,0
G.,0
Söderlund,0
I.,0
Ohlsson,0
T.,0
Boiwe,0
B.-O.,0
Ye,0
X.-C.,0
E.,0
Dekker,0
(1996)Protein,0
Sci.,0
382–390].,0
Kraft,0
J.,0
Tardiff,0
K.S.,0
Krauter,0
L.A.,0
Zakour,0
Methods,0
Enzymol.,0
154,0
1987,0
367,0
382,0
23,0
T.-Z.,0
Keywords,0
threonine,0
dehydrogenase,0
site-directed,0
mutagenesis,0
protein,0
isolation,0
and,0
purification,0
zinc,0
enzyme,0
enzyme,0
active,0
site,0
metal,0
ion,0
activation,0
References,0
REFERENCES,0
1,0
B.D.,0
155,0
1983,0
586,0
592,0
25,0
S.A.,0
Boylan,0
E.E.,0
Dekker,0
J.,0
Biol.,0
Chem.,0
256,0
1981,0
1809,0
1815,0
26,0
K.,0
Weber,0
J.R.,0
Fax:,0
(734),0
763-4581.,0
After,0
it,0
was,0
incubated,0
with,0
1,0
mM,0
Zn2+and,0
then,0
assayed,0
in,0
the,0
presence,0
of,0
15,0
mM,0
Zn2+,0
mutant,0
C38S,0
showed,0
only,0
a,0
trace,0
of,0
enzymatic,0
activity,0
(i.e.,0
0.013,0
unit/mg).,0
Preincubation,0
of,0
mutant,0
C38D,0
with,0
5,0
mM,0
Zn2+,0
Co2+,0
or,0
Cd2+increased,0
its,0
activity,0
57-,0
6-,0
or,0
3-fold,0
respectively;,0
1,0
mM,0
Mn2+halved,0
and,0
0.5,0
mM,0
Hg2+abolished,0
activity.,0
Sun,0
B.V.,0
Plapp,0
J.,0
Mol.,0
Evol.,0
Somerville,0
J.,0
Bacteriol.,0
169,0
1987,0
2611,0
2617,0
21,0
A.R.,0
Johnson,0
E.E.,0
Dekker,0
Arch.,0
Clark-Baldwin,0
A.R.,0
Johnson,0
Y.-W.,0
34,0
1992,0
522,0
535,0
3,0
B.R.,0
Sytkowski,0
Biochem.,0
Biophys.,0
Res.,0
Commun.,0
67,0
1975,0
1494,0
1500,0
34,0
S.A.,0
Boylan,0
E.E.,0
Dekker,0
Biochem.,0
Biophys.,0
Res.,0
Commun.,0
85,0
1978,0
190,0
197,0
3,0
1984,0
357,0
360,0
12,0
M.C.,0
Feiters,0
J.,0
Jeffery,0
Biochemistry,0
28,0
1989,0
7257,0
7262,0
13,0
K.,0
Marcus,0
E.E.,0
Dekker,0
Arch.,0
Zn2+-stimulated,0
mutant,0
C38D,0
showed,0
these,0
properties:,0
apparent,0
substrate,0
activation,0
at,0
low,0
threonine,0
concentrations,0
a,0
maximum,0
activity,0
of,0
27,0
units/mg,0
with,0
20,0
mM,0
threonine,0
and,0
inhibition,0
by,0
high,0
levels,0
of,0
substrate;,0
an,0
activationK,0
d=,0
3,0
mM,0
Zn2+;,0
and,0
a,0
pH,0
optimum,0
of,0
8.4,0
(in,0
contrast,0
to,0
pH,0
10.3,0
for,0
the,0
wild-type,0
enzyme).,0
E.,0
Dekker,0
(1991)J.,0
Biol.,0
Chem.266,0
6086–6092;,0
A.,0
Wong,0
J.,0
Biol.,0
Chem.,0
267,0
1992,0
24989,0
24994,0
14,0
S.,0
Ramaswamy,0
H.,0
Eklund,0
B.V.,0
Plapp,0
Biochemistry,0
33,0
1994,0
5230,0
5237,0
15,0
J.,0
Sambrook,0
E.F.,0
Biochem.,0
Biophys.,0
351,0
1998,0
8,0
16,0
22,0
T.A.,0
Kunkel,0
J.D.,0
R.,0
Johnson,0
and,0
E.,0
Wu,0
S.-L.,0
Somerville,0
Biochim.,0
Biophys.,0
Acta,0
1253,0
1995,0
208,0
214,0
11,0
J.,0
Jeffery,0
J.,0
Chesters,0
C.,0
Mills,0
P.J.,0
Sadler,0
H.,0
Jörnvall,0
EMBO,0
J.,0
was,0
a,0
predoctoral,0
trainee,0
of,0
the,0
National,0
Institutes,0
of,0
Health,0
Research,0
Service,0
Award,0
S-T32-GM07767,0
to,0
the,0
University,0
of,0
Michigan,0
and,0
was,0
a,0
fellow,0
in,0
the,0
Protein,0
Structure,0
and,0
Design,0
Program,0
of,0
the,0
University,0
of,0
Michigan.,0
287,0
1992,0
361,0
365,0
32,0
B.L.,0
Vallee,0
F.L.,0
Hoch,0
Proc.,0
Natl.,0
Acad.,0
Sci.,0
USA,0
41,0
1955,0
327,0
338,0
33,0
C.,0
Veillon,0
A.J.,0
4,0
To,0
whom,0
correspondence,0
and,0
reprint,0
requests,0
should,0
be,0
addressed.,0
Brändén,0
Å.,0
Åkeson,0
J.,0
Mol.,0
Fritsch,0
T.,0
Maniatis,0
Molecular,0
Cloning:,0
A,0
Laboratory,0
Manual,0
1989,0
Cold,0
Spring,0
Harbor,0
Laboratory,0
Press,0
Cold,0
Spring,0
Harbor,0
16,0
F.,0
Sanger,0
S.,0
Nicklen,0
A.R.,0
Coulson,0
Proc.,0
Natl.,0
Acad.,0
Sci.,0
USA,0
74,0
1977,0
5463,0
5467,0
17,0
M.D.,0
Biggin,0
T.J.,0
Leinwand,0
BioTechniques,0
6,0
1988,0
544,0
547,0
19,0
Chen,0
Y.-W.,0
Roberts,0
R.A.,0
Abstract,0
l-Threonine,0
dehydrogenase,0
catalyzes,0
the,0
NAD+-dependent,0
oxidation,0
of,0
threonine,0
forming,0
2-amino-3-ketobutyrate.,0
Epperly,0
E.E.,0
Dekker,0
J.,0
Biol.,0
Chem.,0
264,0
1989,0
5226,0
5232,0
2,0
H.-W.,0
To,0
probe,0
its,0
function,0
Cys-38,0
was,0
changed,0
to,0
Ser,0
Asp,0
and,0
Glu,0
by,0
site-directed,0
mutagenesis.,0
Chemical,0
modification,0
of,0
Cys-38,0
ofEscherichia,0
colithreonine,0
dehydrogenase,0
whose,0
residue,0
aligns,0
with,0
the,0
catalytic,0
zinc-binding,0
residue,0
Cys-46,0
of,0
related,0
alcohol/polyol,0
dehydrogenases,0
inactivates,0
the,0
enzyme,0
[B.,0
A.R.J.,0
Klinman,0
K.,0
Welsh,0
Biochem.,0
Biophys.,0
Res.,0
Commun.,0
70,0
1976,0
878,0
884,0
30,0
A.J.,0
1992,0
University,0
of,0
Michigan,0
Ann,0
Arbor,0
MI,0
20,0
P.D.,0
Having,0
a,0
negatively,0
charged,0
residue,0
like,0
Asp,0
in,0
this,0
position,0
allows,0
the,0
binding,0
of,0
a,0
catalytic,0
Zn2+ion,0
which,0
enhances,0
activity,0
with,0
threonine,0
and,0
reduces,0
activity,0
with,0
substrate,0
analogs.,0
In,0
the,0
absence,0
of,0
added,0
metal,0
ions,0
wild-type,0
enzyme,0
similarly,0
uses,0
substrates,0
other,0
than,0
threonine,0
and,0
shows,0
a,0
dramatic,0
increase,0
in,0
activity,0
with,0
only,0
threonine,0
when,0
stimulated,0
by,0
either,0
Cd2+or,0
Mn2+;,0
added,0
Zn2+has,0
no,0
effect,0
on,0
activity,0
with,0
threonine.,0
Hobert,0
P.,0
Datta,0
J.,0
Bacteriol.,0
serial,0
JL,0
272380,0
291210,0
291847,0
291849,0
291857,0
31,0
Archives,0
of,0
Biochemistry,0
and,0
Biophysics,0
ARCHIVESBIOCHEMISTRYBIOPHYSICS,0
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articleinfo,0
articletitlenorm,0
authfirstinitialnorm,0
authfirstsurnamenorm,0
cid,0
cids,0
contenttype,0
copyright,0
crossmark,0
dateloaded,0
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datesearch,0
datesort,0
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dco,0
docsubtype,0
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webpdf,0
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358,0
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3,0
211,0
221,0
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221,0
19981015,0
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October,0
1998,0
1998-10-15,0
1998,0
converted-article,0
fla,0
Copyright,0
©,0
1998,0
Academic,0
Press.,0
Mutant,0
C38S,0
was,0
catalytically,0
inactive,0
but,0
mutant,0
C38D,0
had,0
a,0
specific,0
activity,0
of,0
0.2,0
unit/mg,0
a,0
level,0