Look up holoprotein in Wiktionary, the free dictionary.
A holoprotein or conjugated protein is an apoprotein combined with its prosthetic group.[1]
Some enzymes do not need additional components to show full activity. Others require non-protein molecules called cofactors to be bound for activity.[2] Cofactors can be either inorganic (e.g., metal ions and iron-sulfur clusters) or organic compounds (e.g., flavin and heme). Organic cofactors can be either coenzymes, which are released from the enzyme's active site during the reaction, or prosthetic groups, which are tightly bound to an enzyme. Organic prosthetic groups can be covalently bound (e.g., biotin in enzymes such as pyruvate carboxylase).[3]
An example of an enzyme that contains a cofactor is carbonic anhydrase, which has a zinc cofactor bound as part of its active site.[4] These tightly bound ions or molecules are usually found in the active site and are involved in catalysis.[5]: 8.1.1 For example, flavin and heme cofactors are often involved in redox reactions.[5]: 17
Enzymes that require a cofactor but do not have one bound are called apoenzymes or apoproteins. An enzyme together with the cofactor(s) required for activity is called a holoenzyme (or haloenzyme). The term holoenzyme can also be applied to enzymes that contain multiple protein subunits, such as the DNA polymerases; here the holoenzyme is the complete complex containing all the subunits needed for activity.[5]: 8.1.1
^"Holoprotein". Farlex Partner Medical Dictionary. 2012.
^de Bolster M (1997). "Glossary of Terms Used in Bioinorganic Chemistry: Cofactor". International Union of Pure and Applied Chemistry. Archived from the original on 21 January 2017. Retrieved 30 October 2007.
^Chapman-Smith A, Cronan JE (1999). "The enzymatic biotinylation of proteins: a post-translational modification of exceptional specificity". Trends Biochem. Sci. 24 (9): 359–63. doi:10.1016/s0968-0004(99)01438-3. PMID 10470036.
^Fisher Z, Hernandez Prada JA, Tu C, Duda D, Yoshioka C, An H, Govindasamy L, Silverman DN, McKenna R (February 2005). "Structural and kinetic characterization of active-site histidine as a proton shuttle in catalysis by human carbonic anhydrase II". Biochemistry. 44 (4): 1097–115. doi:10.1021/bi0480279. PMID 15667203.
^ abcStryer L, Berg JM, Tymoczko JL (2002). Biochemistry (5th ed.). San Francisco: W.H. Freeman. ISBN 0-7167-4955-6.
Look up holoprotein in Wiktionary, the free dictionary. A holoprotein or conjugated protein is an apoprotein combined with its prosthetic group. Some...
confused with the cosubstrate that binds to the enzyme apoenzyme (either a holoprotein or heteroprotein) by non-covalent binding a non-protein (non-amino acid)...
dissociate from the holoprotein, cytochrome c, compared with the more easily dissociated heme B that may dissociate from the holoprotein, the heme-protein...
heat-resistant glycoprotein found to be a trypsin inhibitor. Lysozyme is a holoprotein which can lyse the wall of certain Gram-positive bacteria and is found...
"Bacterial heme synthesis is required for expression of the leghemoglobin holoprotein but not the apoprotein in soybean root nodules". Proceedings of the National...
a synthetic cofactor, what must first occur is the denaturing of the holoprotein to remove the heme. The apoprotein is then rebuilt with the cofactor...
apoprotein (without bound retinal). When an opsin binds retinal to form a holoprotein, it is referred to as Retinylidene protein. However, the distinction...
Friedrich Kühne (1837–1900). When George Wald discovered that rhodopsin is a holoprotein, consisting of retinal and an apoprotein, he called it opsin, which today...
enzyme, is synthesized in the Pr form. Upon binding the chromophore, the holoprotein, an apoprotein combined with its prosthetic group, becomes sensitive...
in 2008 for their work on green fluorescent proteins. Aequorin is a holoprotein composed of two distinct units, the apoprotein that is called apoaequorin...
undecylprodigiosin starts with PCP apoprotein which is transformed into the holoprotein using acetyl CoA and PPtase then adenylation occurs utilizing L-proline...
depth gradients based on the maximal absorption-tuning of the particular holoprotein sequence; this is mainly due to the electromagnetic absorption by water...
non-toxic, but it magnifies the effects of pedoxin. When combined into the holoprotein peditoxin, even low doses resulted in anaphylaxis-like shock and death...
cytochrome c oxidase), enable subunits 1 and 2 to be incorporated into the holoprotein. This gene is the human homolog to the yeast SCO1 gene. It is predominantly...
2007.04.005. PMID 17512176. Perrett HP, et al. (2007). "Disparity in holoprotein/apoprotein ratios of different standards used for immunoquantification...
isoform-specific inhibitory domain regulates the LHX3 LIM homeodomain factor holoprotein and the production of a functional alternate translation form". J. Biol...
that are necessary for guanine nucleotide exchange activity and eIF2B holoprotein formation". Biochimica et Biophysica Acta. 1492 (1): 56–62. doi:10...
that are necessary for guanine nucleotide exchange activity and eIF2B holoprotein formation". Biochim. Biophys. Acta. 1492 (1): 56–62. doi:10.1016/S0167-4781(00)00062-2...
that are necessary for guanine nucleotide exchange activity and eIF2B holoprotein formation". Biochim. Biophys. Acta. 1492 (1): 56–62. doi:10.1016/S0167-4781(00)00062-2...
that are necessary for guanine nucleotide exchange activity and eIF2B holoprotein formation". Biochim. Biophys. Acta. 1492 (1): 56–62. doi:10.1016/S0167-4781(00)00062-2...
against multipass membrane protein substrate cleaving the presenilin 1 holoprotein". FEBS Lett. 557 (1–3): 185–92. doi:10.1016/S0014-5793(03)01489-3. PMID 14741365...
that are necessary for guanine nucleotide exchange activity and eIF2B holoprotein formation". Biochim. Biophys. Acta. 1492 (1): 56–62. doi:10.1016/S0167-4781(00)00062-2...
Mori H, Akagawa K (Aug 2004). "Syntaxin 5 interacts with presenilin holoproteins, but not with their N- or C-terminal fragments, and affects beta-amyloid...
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