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 …

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 …

Isopentenyl-diphosphate isomerases in human and mouse: evolutionary analysis of a mammalian gene duplication

R Breitling, D Laubner, D Clizbe, J Adamski… - Journal of molecular …, 2003 - Springer
Isopentenyl diphosphate isomerase (IDI) activates isopentenyl diphosphate (IPP) for
polymerization by converting it to its highly nucleophilic isomer dimethylallyl diphosphate …

Crystal structure and mechanism of action of the N6-methyladenine-dependent type IIM restriction endonuclease R. DpnI

W Siwek, H Czapinska, M Bochtler… - Nucleic acids …, 2012 - academic.oup.com
DNA methylation-dependent restriction enzymes have many applications in genetic
engineering and in the analysis of the epigenetic state of eukaryotic genomes. Nevertheless …

Isolation of Schizosaccharomyces pombe isopentenyl diphosphate isomerase cDNA clones by complementation and synthesis of the enzyme in Escherichia coli

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 …

Structure and function of the antibiotic resistance-mediating methyltransferase AviRb from Streptomyces viridochromogenes

TG Mosbacher, A Bechthold, GE Schulz - Journal of molecular biology, 2005 - Elsevier
The emergence of antibiotic-resistant bacterial strains is a widespread problem in medical
practice and drug design, and each case requires the elucidation of the underlying …

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 …

A structural basis for the allosteric regulation of non‐hydrolysing UDP‐GlcNAc 2‐epimerases

LM Velloso, SS Bhaskaran, R Schuch, VA Fischetti… - EMBO …, 2008 - embopress.org
The non‐hydrolysing bacterial UDP‐N‐acetylglucosamine 2‐epimerase (UDP‐GlcNAc 2‐
epimerase) catalyses the conversion of UDP‐GlcNAc into UDP‐N‐acetylmannosamine, an …

A family divided: distinct structural and mechanistic features of the SpoU-TrmD (SPOUT) methyltransferase superfamily

A Krishnamohan, JE Jackman - Biochemistry, 2018 - ACS Publications
The SPOUT family of enzymes makes up the second largest of seven structurally distinct
groups of methyltransferases and is named after two evolutionarily related RNA …

Identification of a Catalytic Aspartyl Residue ofd-Ribulose 5-Phosphate 3-Epimerase by Site-directed Mutagenesis

YR Chen, FW Larimer, EH Serpersu… - Journal of Biological …, 1999 - ASBMB
Guided by comparative sequence considerations, we have examined the possibility of a
catalytic role of Asp 186 of d-ribulose 5-phosphate epimerase by site-directed mutagenesis …