Type II isopentenyl diphosphate isomerase: irreversible inactivation by covalent modification of flavin

SC Rothman, JB Johnston, S Lee… - Journal of the …, 2008 - ACS Publications
Isopentenyl diphosphate isomerase (IDI) catalyzes the interconversion of isopentenyl
diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), the basic building blocks of …

Structure of Thermus thermophilus type 2 isopentenyl diphosphate isomerase inferred from crystallography and molecular dynamics

J de Ruyck, SC Rothman, CD Poulter… - … and biophysical research …, 2005 - Elsevier
Crystal structures of Thermus thermophilus and Bacillus subtilis type 2 IPP isomerases were
combined to generate an almost complete model of the FMN-bound structure of the enzyme …

Structure of the reduced disulfide-bond isomerase DsbC from Escherichia coli

K Banaszak, I Mechin, G Frost… - … Section D: Biological …, 2004 - scripts.iucr.org
Disufide-bond isomerase (DsbC) plays a crucial role in folding periplasmically excreted
bacterial proteins. The crystal structure of the reduced form of DsbC is presented. The pair of …

Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase

JS Weissman, PS Kimt - Nature, 1993 - nature.com
Abstract PROTEIN disulphide isomerase (PDI) 1, 2 is a highly abundant and ubiquitous
eukaryotic protein that is essential for viability in yeast3, 4. Although PDI is thought to …

Crystallization and preliminary X-ray diffraction analysis of MspI restriction endonuclease in complex with its cognate DNA

TJ O'Loughlin, Q Xu, RB Kucera, LF Dorner… - … Section D: Biological …, 2000 - scripts.iucr.org
The MspI restriction endonuclease is a type II restriction enzyme. Unlike all other restriction
enzymes with known structures, MspI recognizes the palindromic tetranucleotide sequence …

Crystal structure of human L‐isoaspartyl‐O‐methyl‐transferase with S‐adenosyl homocysteine at 1.6‐Å resolution and modeling of an isoaspartyl‐containing peptide …

CD Smith, M Carson, AM Friedman… - Protein …, 2002 - Wiley Online Library
Spontaneous formation of isoaspartyl residues (isoAsp) disrupts the structure and function of
many normal proteins. Protein isoaspartyl methyltransferase (PIMT) reverts many isoAsp …

Analyzing the functional organization of a novel restriction modification system, the BcgI system

H Kong - Journal of molecular biology, 1998 - Elsevier
BcgI is a novel, multi-subunit, restriction-modification (RM) system that differs from all the
other types of RM system in its genetic and functional organization. The holoenzyme …

Escherichia coli Type I Isopentenyl Diphosphate Isomerase:  Structural and Catalytic Roles for Divalent Metals

S Lee, CD Poulter - Journal of the American Chemical Society, 2006 - ACS Publications
Isopentenyl diphosphate isomerase (IDI) catalyzes the essential conversion of isopentenyl
diphosphate (IPP) to dimethylallyl diphosphate (DMAPP) in the mevalonate entry into the …

Molecular Structure of the NADH/UDP-glucose Abortive Complex of UDP-galactose 4-Epimerase from Escherichia coli:  Implications for the Catalytic Mechanism,

JB Thoden, PA Frey, HM Holden - Biochemistry, 1996 - ACS Publications
UDP-galactose 4-epimerase is one of three enzymes in the metabolic pathway that converts
galactose into glucose1-phosphate. Specifically this enzyme catalyzes the interconversion …

[HTML][HTML] Isolation of Schizosaccharomyces pombe isopentenyl diphosphate isomerase cDNA clones by complementation and synthesis of the enzyme in Escherichia …

FM Hahn, CD Poulter - Journal of Biological Chemistry, 1995 - ASBMB
Isopentenyl diphosphate (IPP) isomerase catalyzes an essential activation step in the
isoprene biosynthetic pathway. The Saccharomyces cerevisiae gene for IPP isomerase …