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isomerase

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isomerase

 [i-som´er-ās]
a major class of enzymes comprising those that catalyze the process of isomerization, such as the interconversion of aldoses and ketoses.
Miller-Keane Encyclopedia and Dictionary of Medicine, Nursing, and Allied Health, Seventh Edition. © 2003 by Saunders, an imprint of Elsevier, Inc. All rights reserved.

i·som·er·ase

(ī-som'ĕr-ās),
A class of enzymes catalyzing the conversion of a substance to an isomeric form, for example, glucosephosphate isomerase.
Farlex Partner Medical Dictionary © Farlex 2012

isomerase

(ī-sŏm′ə-rās′)
n.
Any of a group of enzymes that catalyze the conversion of one isomer into another.
The American Heritage® Medical Dictionary Copyright © 2007, 2004 by Houghton Mifflin Company. Published by Houghton Mifflin Company. All rights reserved.

i·som·er·ase

(ī-som'ĕr-ās)
A class of enzymes (EC class 5) catalyzing the conversion of a substance to an isomeric form.
Medical Dictionary for the Health Professions and Nursing © Farlex 2012

isomerase

a group of enzymes that converts organic compounds from D- to L-, or L- to D-forms.
Collins Dictionary of Biology, 3rd ed. © W. G. Hale, V. A. Saunders, J. P. Margham 2005
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References in periodicals archive
Key words: xylose isomerases thermotogales hyperthermophiles INTRODUCTION
IPP isomerase (EC 5.3.3.2) catalyzes an essential reaction in the MVA pathway by converting IPP to DMAPP.
Proteasomal degradation of human peptidyl prolyl isomerase pin1-pointing phosphor Bcl2 toward dephosphorylation.
Maleylacetoacetate isomerase (MAAI/GSTZ)-deficient mice reveal a glutathione-dependent nonenzymatic bypass in tyrosine catabolism.
In a recent study using the symbiotic tropical sea anemone Aiptasia pulchella, one of the genes that was found highly expressed in symbiotic anemones was identified as a peptydylprolyl cis-trans isomerase (PPIase) of the cyclophilin family (Kuo et al., 2004).
Jacob et al., "Structure of bacterial glutathione-S-transferase maleyl pyruvate isomerase and implications for mechanism of isomerisation," Journal of Molecular Biology, vol.
The sequence has the similar characters for basic structural function of Cyclophilin A, the cyclophilin type peptidyl-prolylcis-trans isomerases signature and conserved amino acid residues are similar with already investigated CypA in different species (Howard et al., 2003; Piotukh et al., 2005; Eisenmesser et al., 2002; Qiu et al., 2009; Chen et al., 2011).
Over 30% of known enzymes are metalloenzymes, covering all major enzyme classes: oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases.
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