office: 973.353.5470
Research Interests
Research in our laboratories focuses on the structure,
regulation, mechanism of action, and folding of two groups of enzymes.
Our research on thiamin diphosphate (the vitamin B1 coenzyme)-dependent
enzymes has followed a dual approach. Part of our group is studying how
a-keto acid decarboxylascs work, including both nonoxidative and oxidative
functions. Questions being asked include determining the 3-D structure
of the protein, the conformation and activation of the coenzymes in catalysis,
the nature of proton transfer events in catalysis, and the mechanism of
electron and group transfer in the oxidative processes. Tools used in these
studies include high resolution X-ray crystallography (pyruvate decarboxylase,
the simplest of these enzymes was solved to a resolution of 2.3A; the E1
subunit of the E. coli pyruvate dehydrogenase multienzyme complex to 1.85Å),
nuclear magnetic resonance spectroscopy, molecular genetics to change amino
acids in the structure to establish structure-function relationships, steady-state
and pre-steady-state kinetics, and immunochemical methods. Our enzyme studies
are being complemented with model organic chemical studies, in which the
elementary steps of the multi-step enzymatic reactions are being modeled.
From such chemical models, one can learn which step and by how much the
enzyme must accelerate.
Our research on serine proteases has two principal aims.
First, we are attempting to define the active center electronic structure
in the enzymes in the absence and in the presence of both synthetic and
protein protease inhibitors. From these studies, a picture is emerging
that can differentiate ground-state vs. transition-state vs. acyl-enzyme
type inhibitors, providing a convenient tool for drug design. The second
part of our research focuses on the varied roles of the pro-sequence in
enzymes expressed as pre-pro-proteins. Subtilisin, an alkaline bacterial
protease, is the model being used (27.5 kDa), since its pro-sequence (8.5
kDa, 77 amino acids) has been shown to be important both for folding of
FRANK JORDAN
Rutgers Board of Governors Professor of Chemistry
Director, Program in Cellular and Molecular Biodynamics
Organic Chemistry, Enzyme Structures, Folding Mechanisms
Ph.D., 1967, University of Pennsylvania
Postdoctoral fellowships (1967-1968) Sorbonne and (1968-1970)
Harvard University
1970 joined Rutgers-Newark faculty.
Participant in the Training
Program in Cellular and Molecular Biodynamics
lab: 973.353.5039
email: frjordan@newark.rutgers.edu
Representative
Publications
Research Interests
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