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Jo
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MERTON FRANKLIN UTTER
March23, 1917-November2S, 1980
BY HARLAND G. WOOD AND RICHARD W. HANSON
THE MOST SIGNIFICANT CONTRIBUTION to biochem-
istry made by Merton F. Utter was his demonstration that
certain reactions of gluconeogenesis differ from those of gly-
colysis. For many years it was widely helcl that the synthesis
of glucose (gluconeogenesis) in mammalian liver occurs by
reversal of the EmbJen-Meyerhof pathway by which glucose
is converted to pyruvate and lactate (glycolysis). Merton Utter
and his coworkers shower! that this concept is incorrect. They
discovered phosphoenolpyruvate carboxykinase and pyru-
vate carboxylase, two enzymes that in concert convert pyru-
vate to phosphoenolpyruvate by a sequence that differs from
the glycolytic pathway.
This discovery opener! new vistas in the study of metab-
olism, and over the past decade it has become evident that
the two enzymes discovered by fitter anct coworkers are also
important in the regulation of both carbohydrate and lipic}
metabolism. Utter, together with Dr. Bruce Keech, clemon-
strated that acetyI-CoA regulates the activity of pyruvate car-
boxylase, thus providing one of the first examples of allo
steric control of an enzyme. Furthermore, the rate-limiting
step in gluconeogenesis is catalyzed by phosphoenolpyruvate
carboxykinase, whose levels in mammalian liver and kiciney
are regulated by insulin, glucagon, epinephrine, and gluco
475
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476
BIOGRAPHICAL MEMOIRS
corticoids. This enzyme has been extensively studied as a
mode} for the action of these hormones on gene expression
in mammalian tissues. Prior to his death, Utter's studies had
increasingly centered on the interface between disease pro-
cesses and basic biochemistry. His laboratory was considered
one of the leading centers studying inborn errors in the me-
tabolism of pyruvate, and his collaboration was constantly
sought by clinical investigators anxious to verify the absence
of specific enzymes in patients suffering from various cTis-
eases. The scope of his science was broad. He stooct for pre-
cise and excellent experiments, and his advice was sought on
a wide variety of subjects. His was a keen intellect, but he was
always moclest ant! friendly, and was possessed of a sharp wit.
Merton Utter's interests extendect to all aspects of life: sci-
ence, sports, politics, literature, ant! the arts.
UTTER S BACKGROUND
Merton Franklin Utter was born at Westboro, Missouri,
on March 23, 1917. His parents were Merton Franklin Utter,
Sr., anct Gertrude R. McMichae} Utter. His father and grand-
parents, Mr. and Mrs. L. P. Utter, had moved to Missouri
from Trempealeau, Wisconsin. His maternal grandparents
were Mr. and Mrs. A. R. McMichae] of Coin, Iowa. Most of
his ancestors came to New England anct New York from the
British Isles in the seventeenth and early eighteenth centu-
ries. When he was a few months old, Merton's parents moved
to New Market, Iowa, where his father was a banker, and his
early school years were spent there. His mother gave piano
lessons and played piano and organ for churches most of her
life. It was from her that Merton acquired a deep and lifelong
love of music.
In 1930, when Merton was in the eighth gracle, the family
moved to Coin, Iowa. He gracluated from the high school
there in 1934 and entered Simpson College at Inclianola,
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MERTON FRANKLIN UTTER
477
Iowa. The cleath of his father in an auto accident in the sum-
mer of ~ 935 interrupter! his college studies briefly, but
he graduated from Simpson in 193S, supporting himself
through scholarship aid and by managing the campus book-
store. He was a fine athlete and excelled in track and basket-
balI. At Simpson he clistinguishecl himself in the field of
chemistry, and on the advice of his professor he enrolled in
graduate school at Iowa State University at Ames. In 1942,
with the sect of fellowships, he was able to complete the work
for his Ph.D. degree, which he received in microbiology in
the laboratory of Dr. C. H. Werkman. In that year he was
appointee] an instructor in bacteriology.
On September 2, 1939, while at Ames, he married Mar-
jorie ManifoIcI, whom he had known since high school. Mem-
bers of her family were also longtime residents of Coin and
vicinity (Page County). In [944 the Utters moved to Minne-
apolis, where he was assistant professor of physiological
chemistry at the University of Minnesota, and in 1946 they
mover! to ClevelancI, Ohio, where he was appointed associate
professor of biochemistry at Western Reserve University
School of Medicine. A son, Douglas Max Utter, was born on
December 8, 1950. In 1956 Merton Utter was promoted to
professor, and in 1965 he became chairman of the Biochem-
istry Department ant] continued in that position until 1976.
Thereafter he clevoted his full time to research and teaching
in the Department of Biochemistry.
He and his family spent three years abroad on leave of
absence from Case Western Reserve University. In 1953, he
traveled with his family to Aclelaicle, Australia, where he was
a Fulbright Fellow at the University of South Australia. In
1960 he served as visiting professor at Oxford University in
Englanc! and in 1968 at the University of Leicester. Recently,
Sir Hans Kornberg reflected on the year spent by the Utter
family in Leicester.
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478
BIOGRAPHICAL MEMOIRS
it seemeci appropriate that 7 years later they, Marge, Mert and Doug,
should come back to Leicester. They lived around the corner from us and
every morning either Mert would come and ring my doorbell and I would
hastily wipe the last vestiges of breakfast toast off my face and then walk
with him across the park; or I would call for him on wet days in a mon-
strous car, a 12 seater. When you walk with someone for a whole year you
get to know him pretty well. Mert had a tremendous interest in the com-
parative side of biological phenomena. We used to talk about this sort of
thing trying to discover the reason why, for example, you have a perfectly
good enzyme, pyruvate carboxylase, which a perfectly good bacteria like
E. cold should resolutely refuse to use, and instead it used PEP carboxylase
but used the same mechanism of control. And we would play games like
what if, and supposing that. This to me brought out the one feature of my
association with Mert which I remember distinctly with the strongest af-
fection. He was a tremendous person to be with because he would toss
ideas around and he, like me, had this fatal fascination for playing on
words. We would usually end our walks giggling helplessly as we went into
the department where they must have thought us ready for certification
as lunatics.
A SUMMARY OF HIS RESEARCH
Early Research. Utter's first scientific paper was published
in the Iowa State College journal of Science (1940) and was en-
titled "The Preparation of an Active Juice from Bacteria."
Utter was always modest and unpretentious. A title such as,
"A Unique and New Procedure for Preparation of Active En-
zymes from Bacteria" would have been more to the point and
sounded more sophisticated, but that was not his style. The
solubilization of bacterial enzymes was a significant accom-
plishment. At that time, soluble enzyme systems capable of
fermenting carbohydrates hac! not been demonstrated in
bacteria, ant] consideration of their intermediary metabolism
was in large part based on what was known from studies of
enzymes from yeast anct animal tissue.
Those were the "horse and buggy" clays of biochemistry.
The citric acid cycle had just been described by Krebs, and
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MERTON FRANKLIN UTTER
479
many details of the Embden-Meyerhof pathway were not
completely understood. There were no commercial sources
of enzymes or of coenzymes such as adenosinetriphosphate
(ATP) and nicotinamide diphosphate and triphosphate
(NAD and NADP). It was a time of "do-it-yourself or go with-
out." To solubilize enzymes, bacteria were mixed with ground
glass and the mixture was forced between the interface of
two tightly interfitting cones. For this purpose, a glass tube
was sealed to the neck of one ErIenmeyer flask and the bot-
tom of the flask was cut off. A second ErIenmeyer flask was
sealed off at the neck so that it fit inside the open end of the
first Erienmeyer flask. The inner flask was attached to a mo-
tor to cause it to rotate within the outer flask. A mixture of
the bacteria, together with ground glass, was placed in the
tube of the outer flask, and the mixture was forced, using
considerable effort, from the tube between the rotating cones
using a plunger. These were the depression years, so if a
beaker was broken, it was saved and the glass was put in a
ball mill to replenish the ground glass. This procedure for
the preparation of bacterial enzymes was used for many years
by researchers in C. H. Werkman's department.
At about the same time, a mass spectrometer for mea-
surement of i3C was being constructed by the group in the
laboratory, as well as a thermal diffusion column five stories
high for concentration of this stable isotope. It was the in-
genuity and hard work of graduate students such as Merton
Utter that made the laboratory of C. H. Werkman, which was
situated in the middle of the farm belt of Iowa, a leading
center for study of microbial metabolism.
This is the environment in which Merton Utter started his
research. He had a nine-month fellowship that paid $50
monthly. His wife Marjorie worked as a secretary with Dr.
Theodore Schultz in the Department of Economics at Iowa
State College, now Iowa State University. Interestingly, Dr.
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BIOGRAPHICAL MEMOIRS
Schultz, who by then had moved to Chicago, was a winner of
the Nobel Prize in Economics in 1979.
Merton Utter's research was truly pioneering. In 1941 a
paper was publishecI in the journal of Bacteriology entitled
"The Occurrence of the Aldolase anc! Isomerase Equilibria
in Bacterial Metabolism." Alclolase and isomerase are two im-
portant enzymes of carbohydrate metabolism. There were
two more papers publishecI in the Journal of Biological Chem-
istry in 1942: "Effect of Metal ions on the Reactions of Phos-
phopyruvate by Escherichia coli" and "The Dissimilation of
Phosphoglyceric Acid by Escherichia coli." Phosphoglyceric
acid hac! been shown at that time to be a key compound in
the metabolism of carbohydrate by yeast and mammalian tis-
s-ues. In 1943 Utter published "The Role of Phosphate in the
Anaerobic Dissimilation of Pyruvic Acid" and in 1944 the
"Formation and Reactions of Acety~phosphate in Escherichia
coli" and "Reversibility of the Phosphorociastic Split of Pyr-
uvate." (At that time, Fritz Lipmann had just discoverecI the
role of acety~phosphate in metabolism.) Anyone who is fa-
miliar with the history of biochemistry recognizes from the
titles that Merton Utter's early work was at the forefront of
biochemistry, just as it has been at the forefront of carbohy-
ctrate metabolism to this clay. Methods of isolation of enzymes
and study of their properties were in their infancy. Utter's
studies helped to show that bacteria share similar metabolic
pathways with mammals and that all forms of life exist in
large part by the same biochemical processes. Soon bacteria
were to become the major subject for study of intermediary
metabolism and molecular biology.
Studies on Fixation of CO2. The fixation of CO2 by hetero-
trophic organisms was discovered by H. G. Wood and C. H.
Werkman in 1936. Later they proposed that the fixation oc-
curred as follows:
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MERTON FRANKLIN UTTER
*CO2 + CH3 CO COOH > HOO*C CH2 CO COOH
481
This reaction became known as the Wood and Werkman re-
action. It was not until 194X, however, that S. Ochoa, A. H.
MehIer, and A. Kornberg purified an enzyme that fixed CO2
to form a dicarboxylic acid. Subsequently, the enzyme was
named the malic enzyme and shown to catalyze the following
reaction:
malic enzyme
CON + pyruvate + NADPH ~ ~ malate + NADP
Following this discovery, Ochoa and collaborators suggested
that this enzyme catalyzed the primary reaction in the fixa-
tion of CO2 and that oxalacetate is former! by coupling the
following two reactions:
malic enzyme
CO' + pyruvate + NADPH ~ ~ malate + NADP
malic dehydrogenase
Malate + NAD _ - oxalacetate + NADH
Sum: CO, + pyruvate + NADPH + NAD ~ oxalacetate +
NADP +
NADH
Ephraim Racker summarized the status of work in this field
at a meeting on CO2 fixation in 1950, when he proposed a
toast to the "wouldn't work reaction."
Although the enzymatic basis for the Wood and Werkman
reaction continued to be elusive, Utter and K. Kurahashi
showed that chicken liver forms oxalacetate without the in-
volvement of malic enzyme. They isolated a new enzyme,
.
P-enolpyruvate carboxykinase, which catalyzes the formation
of oxalacetate with fixation of CO2, using guanosine di- and
triphosphate (GDP and GTP) as high-energy intermecliates:
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482
BIOGRAPHICAL MEMOIRS
P-ellolpyrtl vale
cart~oxykinase
P-enolpyruvate + COW + GDP ~
oxalacetate + GTP
Utters Discovery of the Mechanism of Conversion of Pyravate to
P-enolpyravate. It was the finding of P-enolpyruvate carboxy-
kinase that launched Utter into the studies of gluconeoge-
nesis. He was aware that because of the high, negative free
energy change it was
r. ~
unlikely that P-enolpyruvate was
formed trom pyruvate by a simple reversal of the pyruvate
. .
. Gnash reaction.
pyruvat e
kinase
P-enolpyruvate + ADP ~ pyruvate + ATP
(AG° = - 7 kcal/mole)
As a possible solution, both H. A. Krebs and Utter (1954)
inclepenclently proposed that pyruvate might be converted
to P-enolpyruvate by the combined action of the malic en-
zyme and P-enolpyruvate carboxykinase by the following se-
quence:
malic enzyme
Pyruvate + CO2 + NADPH ~ ~ malate + NADP
malic dehydrogenase
Malate + NAD - oxalacetate + NADH
P-er~olpyruvate
Oxalacetate + GTP ~ - P-enolpyruvate + GDP + CO2
carboxykinase
Sum: Pyruvate + GTP + NADPH + NAD >
P-enolpyruvate + GDP + NADP + NADH
The thermodynamics of this sequence are not particularly
favorable, but by coupling the oxidation of NADH to other
reactions it was considered possible to maintain a high ratio
of NADPH/NAD, thereby favoring the synthesis of the
P-enolpyruvate.
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MERTON FRANKLIN UTTER
483
It was an investigation of the above reaction sequence that
lecl to the discovery of the major anaplerotic enzyme, pyru-
vate carboxykinase. Utter and coworkers then fount} that mi-
tochonciria from chicken liver contained only trace amounts
of either pyruvic kinase or malic enzyme, but they could still
form significant amounts of P-enolpyruvate from pyruvate.
These experiments provider! the first clear evidence that nei-
ther of these enzymes was required for the net synthesis of
P-enolpyruvate. Since Utter knew that P-enolpyruvate could
be formed from oxalacetate, it was natural to look for an
enzyme that could form oxalacetate from pyruvate. In 1963
Utter and D. B. Keech fount! such an enzyme in the mito-
chondria of chicken liver (later named Pyruvate carboxylase),
which catalyzed the direct carboxylation of pyruvate. Utter
tract thus found the enzymatic basis of the "wouldn't work re-
action," twenty-five years after it had been postulated as a
possible mechanism for the formation of dicarboxylic acids
by CO2 fixation. Pyruvate carboxylase, when coupled with P-
enolpyruvate carboxykinase, catalyzecI the formation of P-
enolpyruvate as illustrated below.
Pyruvate carboxylase
Pyruvate + CO2 + ATP ~-
oxalacetate + ADP + P
P-er~olpyravate
Oxalacetate + GTP ~ ~ P-enolpyruvate + CON + GDP
carboxy k'nase
i
Sum: Pyruvate + ATP + GTP ~ P-enolpyruvate +
ADP + GDP + Pi
This sequence is energetically favorable because it combines
cleavage of two high-energy phosphates from ATP and GTP
to drive the overall synthesis of P-enolpyruvate. A beautiful
summary of this research was published in a 1963 article by
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484
BIOGRAPHICAL MEMOIRS
Utter in the Iowa State College Journal of Science, which con-
tained a compilation of papers by C. H. Werkman's students.
Toclay this pathway of P-enolpyruvate formation from py-
ruvate is wiclely held as the key, pacesetting step in gluconeo-
genesis. The degree of the regulation of the two enzymes in
this sequence, pyruvate carboxylase and P-enolpyruvate car-
boxykinase, now serves as a mocle] for control of metabolic
pathways and remains a major legacy of Merton Utter's scien-
tific work.
Structure of Biotin Enzymes. One portion of Utter's research
that hac! a large effect was his 1966 study, in collaboration
with R. C. Valentine, N. C. Wrigley, M. C. Scrutton, and I. l.
arias, using electron microscopy to determine the structure
of pyruvate carboxylase from chicken liver. This was one of
the earliest applications of electron microscopy for investi-
gation of the quaternary structure of enzymes. Negative
staining techniques showed square-planar tetramers with
vivict clarity. It was these studies that convinced one of us
(H. G. W.) to undertake similar studies with another biotin
enzyme, transcarboxylase, and no doubt inclucect others to
adopt the procedure.
That pyruvate carboxylase was being visualized seemed
compelling. Pyruvate carboxylase was known to contain four
In accord with the observed tetrameric
structure. Also, estimates from the dimensions of the profiles
of the four subunits were in accord with the observer! molec-
ular weight of the enzyme. These square tetramers were ob-
servec! in pyruvate carboxylase preparations from the livers
of a variety of animals, including the chicken, turkey, beef
cattle, ant! calf. In acictition, Gottschalk and coworkers (Eu-
ropean Journal of Biochemistry, 64 ~ ~ 976] :4 ~ I-2 ~ ~ at the Uni-
versity of Gottingen, Federal Republic of Germany, reported
that pyruvate carboxylase of rat liver hac! a square tetramer
shape. Finally and most convincingly, pyruvate carboxylase
biotins, which was
.
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MERTON FRANKLIN UTTER
PROFESSIONAL SOCIETIES
American Society of Biological Chemists
American Association for the Advancement of Science
American Chemical Society
American Society of Microbiologists
Biochemical Society (England)
New York Academy of Sciences
Society of Experimental Biology and Medicine
489
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490
BIOGRAPHICAL MEMOIRS
SELECTED B IBLIOGRAPHY
1940
With W. P. Wiggert, M. Silverman, and C. H. Werkman. Prepara-
tion of an active juice from bacteria. Iowa State Coll. I. Sci.,
14: 179-86.
1941
With C. H. Werkman. Occurrence of the aldolase and isomerase
equilibria in bacterial metabolism. I. Bacteriol., 42 :665-76.
1942
With C. H. Werkman. Effect of metal ions on the reactions of phos-
phopyruvate by Escherichia coli. ]. Biol. Chem., 146:289 -300.
With C. H. Werkman. Dissimilation of phosphoglyceric acid by
Escherichia coli. Biochem. I., 36:485-93.
1943
With C. H. Werkman. Role of phosphate in the anaerobic dissi-
milation of pyruvic acid. Arch. Biochem., 2:491-92.
1944
With C. H. Werkman. Formation and reactions of acetyl phosphate
in Escherichia coli. Arch. Biochem., 4:413-22.
With C. H. Werkman and F. Lipmann. Reversibility of the phos
ohoroclastic solit of pyruvate. }. Biol. Chem., 154:723-24.
1945
With F. Lipmann and C. H. Werkman. Reversibility of the phos-
phoroclastic split of pyruvate. J. Biol. Chem., 158:521-31.
With I. M. Reiner and H. G. Wood. Measurement of anaerobic gly-
colysis in brain as related to poliomyelitis. }. Exp. Med.,82:217-
26.
With H. G. Wood. Fixation of carbon dioxide in oxalacetate by
pigeon liver. I. Biol. Chem., 160:375 -76.
With H. G. Wood and I. M. Reiner. Anaerobic glycolysis in nervous
tissue. }. Biol. Chem., 1 6 1: 1 97-2 1 7.
With G. Kalnitsky and C. H. Werkman. Active enzyme prepara-
tions from bacteria. I. Bacteriol., 49:595 -602.
OCR for page 491
MERTON FRANKLIN UTTER
1946
491
With L. O. Krampitz and C. H. Werkman. Oxidation of acetyl
phosphate and other substrates by Micrococcus Iysodeikticus.
Arch. Biochem., 9:285 -300.
With G. Kalnitsky and C. H. Werkman. Enzymatic nature of cell-
free extracts from bacteria. Arch. Biochem., 9:407-17.
With H. G. Wood. The fixation of carbon dioxide in oxalacetate by
pigeon liver. J. Biol. Chem., 164:455-76.
1950
Mechanism of inhibition of anerobic glycolysis of brain by sodium
ions. I. Biol. Chem., 185 :499-517.
With V. Lorber, H. Rudney, and M. Cook. The enzymatic forma-
tion of citric acid studied with C~4-labeled oxalacetate. }. Biol.
Chem., 185 :689-99.
The mechanism of the fixation of carbon dioxide in dicarboxylic
acids. Brookhaven Natl. Lab. Symp. CO2 Assimilation Reaction,
pp. 37-55.
1951
Interrelationships of oxalacetic and 1-malic acids in carbon dioxide
fixation. I. Biol. Chem., 188:847-63.
Adenosine triphosphate and carbon dioxide fixation. In: Phospho-
rus Metabolism, ed. W. D. McElroy and B. Glass, Vol. 1, pp. 646-
56. Baltimore: The Johns Hopkins Press.
With H. G. Wood. Mechanism of fixation of carbon dioxide by het-
erotrophs and autotrophs. Adv. Enzymol., 12:41-151.
1953
With K. Kurahashi. Mechanism of action of oxalacetic carboxylase
from liver. I. Am. Chem. Soc., 75:758.
1954
With K. Kurahashi. Purification of oxalacetic carboxylase from
chicken liver. }. Biol. Chem., 207:787-802.
With K. Kurahashi and I. A. Rose. Some properties of oxalacetic
carboxylase. I. Biol. Chem., 207:803 -l 9.
With K. Kurahashi. Mechanism of action of oxalacetir carboxylase.
}. Biol. Chem., 207:821-41.
OCR for page 492
492
BIOGRAPHICAL MEMOIRS
1955
With K. Kurahashi. Oxalacetate synthesizing enzyme. Methods En-
zymol., 1:758-63.
1956
With I. L. Graves, B. Vennesland, and R. I. Pennington. The mech-
anism of the reversible carboxylation of phosphoenolpyruvate.
I. Biol. Chem., 233:551-57.
1957
With K. Kurahashi and R. }. Pennington. Nucleotide specificity of
oxalacetic carboxylase. }. Biol. Chem., 226: 1059-75.
With H. E. Swim. Isotopic experimentation with intermediates of
the tricarboxylic acid cycle. Methods Enzymol., 4:584-608.
1958
With D. B. Keech and P. M. Nossal. Oxidative phosphorylation of
subcellular particles from yeast. Biochem. I., 68:431-40.
Carbohydrate metabolism. Annul Rev. Biochem., 27:245-84.
Guanosine and inosine nucleotides. The Enzymes, II:75-88.
1959
The role of CON fixation in carbohydrate utilization and synthesis.
N.Y. Acad. Sci., 72:451-61.
With }. T. McQuate. Equilibrium and kinetic studies of the pyruvic
kinase reaction. }. Biol. Chem., 234:2151-57.
1960
With D. B. Keech. Formation of oxaloacetate from pyruvate and
CON. I. Biol. Chem., 235: PC 17-18.
Nonoxidative carboxylation and decarboxylation. The Enzymes,
V:319-40.
1962
With }. Mendicino. Interaction of soluble and mitochondrial mul-
tienzyme systems in hexose phosphate synthesis. I. Biol. Chem.,
237: 1716-22.
OCR for page 493
MERTON FRANKLIN UTTER
1963
493
Pathways of phosphoenolpyruvate synthesis in glycogenesis. Iowa
State Coll. }. Sci., 38:97-113.
With D. B. Keech. Pyruvate carboxylase. I. Nature of the reaction.
I. Biol. Chem., 238:2603-8.
With D. B. Keech. Pyruvate carboxylase. II. Properties. l. Biol.
Chem., 238:2609 -14.
1964
With D. B. Keech and M. C. Scrutton. A possible role for acetyl
CoA in the control of gluconeogenesis. Adv. Enzyme Regul.,
2:49-68.
With E. A. Duell and S. Inoue. Isolation and properties of intact
mitochondria from spheroplasts of yeast. }. Bacteriol., 88: 1762-
73.
1965
With M. C. Scrutton. Pyruvate carboxylase. III. Some physical and
chemical properties of highly purified enzyme. J. Biol. Chem.,
240: 1-9.
With M. C. Scrutton and D. B. Keech. Pyruvate carboxylase. IV.
Partial reactions and the locus of activation by acetyl coenzyme
A. I. Biol. Chem., 240:574-81.
With M. C. Scrutton. Pyruvate carboxylase. V. Interaction of the
enzyme with adenosine triphosphate. I. Biol. Chem.,
240:3714-23.
With H. G. Wood. The role of CON fixation in metabolism. Essays
Biochem., 1:1-27.
1966
With M. C. Scrutton and A. S. Mildvan. Pyruvate carboxylase. VI
The presence of tightly bound manganese. T. Biol. Chem.
241 :3480-87.
With A. S. Mildvan and M. C. Scrutton. Pyruvate carboxylase. VII
A possible role for tightly bound manganese. I. Biol. Chem.
241 :3488-98.
With R. C. Valentine, N. G. Wrigley, M. C. Scrutton, and I. I. Irias.
OCR for page 494
494
BIOGRAPHICAL MEMOIRS
Pyruvate carboxylase. VIII. The subunit structure as examined
by electron microscopy. Biochemistry, 5:3111-16.
With C. Bernofsky. Mitochondrial isocitrate dehydrogenase from
yeast. I. Biol. Chem., 241:5561-66.
Oxalacetic decarboxylase and related enzymes. Handb. Physiol. Pa-
thol. Chem. Anal., 10:498-502, Berlin: Springer-Verlag.
1967
With C. Bernofsky. Secondary activation effects of mitochondrial
isocitrates dehydrogenases from yeast. Biochim. Biophys. Acta,
132:244-55.
With M. C. Scrutton, M. R. Young, B. Tolbert, I. C. Wallace, ~ I
Irias, and R. C. Valentine. Pyruvate carboxylase. The relation-
ship of enzymic structure to catalytic activity, 7th Internatl.
Cong. Biochem., Tokyo.
1968
With C. Bernofsky. Interconversions of mitochondrial pyridine nu-
cleotides. Science, 159: 1362-63.
The carboxylation of Pyruvate by biotin-enzymes. l. Vitamin,
14:68-76.
With M. C. Scrutton and M. R. Olmsted. Pyruvate carboxylase
from chicken liver. Methods Enzymol., 13:235-49.
With M. R. Young and B. Tolbert. Pyruvate carboxylase from Sac-
charomyces cerevisiae. Methods Enzymol., 13:257-65.
With E. A. Duell and C. Bernofsky. Alterations in the respiratory
enzyme of the mitochondria of growing and resting yeast. In:
Aspects of Yeast Metabolism, ed. A. K. Mills, pp. 197 - 212. Oxford:
Blackwell Scientific Publications.
With M. C. Scruttor~. The regulation of glycolysis and gluconeo-
genesis in animal tissues. Annul Rev. Biochem., 37:249-302.
1969
With M. C. Scrutton. Pyruvate carboxylase. In: Current Topics in
Cellular Regulation, vol. 1, ed. B. L. Horecker and E. R. Stadt-
man, pp. 253-96. New York: Academic Press.
With I. A. Rose, E. L. O'Connell, P. Noce, H. G. Wood, I. M. Wil-
lard, T. C. Cooper, and M. Benziman. Stereochemistry of the
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MERTON FRANKLIN UTTER
495
enzymatic carboxylation of phosphoenolpyruvate. J. Biol.
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With I. }. Irias and M. R. Olmsted. Pyruvate carboxylase. Revers-
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Representative terms from entire chapter:
merton franklin
