holoenzyme

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Related to holoenzyme: apoenzyme

holoenzyme

[hol″o-en´zīm]

the active compound formed by combination of a coenzyme and an apoenzyme.

hol·o·en·zyme

(hol'ō-en'zīm),

A complete enzyme, that is, apoenzyme plus coenzyme, cofactor, metal ion, and/or prosthetic group.

holoenzyme

/holo·en·zyme/ (-en´zīm) the active compound formed by combination of a coenzyme and an apoenzyme.

holoenzyme

(hŏl′ō-ĕn′zīm′, hō′lō-)

An active, complex enzyme consisting of an apoenzyme and a coenzyme.

holoenzyme

[hol′ō·en′zīm]

Etymology: Gk, holos + en, in, zymos, ferment

a complete enzyme-cofactor complex that gives rise to full catalytic activity.

hol·o·en·zyme

(hol'ō-en'zīm)

A complete enzyme, i.e., apoenzyme plus coenzyme, cofactor, metal ion, and/or prosthetic group.

holoenzyme

A complete enzyme that includes its prosthetic coenzyme. An enzyme without its coenzyme is called an apoenzyme.

holoenzyme

an entire conjugated enzyme consisting of a protein component (an apoenzyme) and a nonprotein component (a coenzyme or an activator).

holoenzyme

an enzyme which contains several different subunits and retains some activity even when one or more of the subunits is missing.

References in periodicals archive ?

Another reversible dissociation mechanism regulated by the C subunit underlies the separation of the holoenzyme V1V0 into V1 and V0 subcomplexes, which occurs through the binding of the C subunit and F-actin proximal to the basement membrane of epithelial cells.

An update in the structure, function, and regulation of V-ATPases: the role of the C subunit/Uma atualizacao na estrutura, funcao e regulacao das V-ATPases: o papel das subunidades C

Several domains of pol [gamma]B interact with pol [gamma]A as shown by electron microscopy and the recent pol [gamma] holoenzyme crystal structure.

Mitochondrial disorders of DNA polymerase [gamma] dysfunction: from anatomic to molecular pathology diagnosis

Undoubtedly the regulation of V-ATPases is a highly complex process as it requires the expression of genes encoding the various subunits, assembly and targeting of the V-ATPase holoenzyme to functionally diverse subcellular compartments, and modulation of activity in response to a host of developmental, physiological and environmental stimuli.

V-ATPase in plants: an overview V-ATPase: structure and role in plants

The ultramutated phenotype is attributed to somatic mutations in the exonuclease domain of POLE, which encodes the catalytic and proofreading subunit of the polymerase e holoenzyme that catalyzes leading-strand synthesis during DNA replication and regulates cell cycle progression, chromatin remodeling, and DNA repair (59).

The emerging genomic landscape of endometrial cancer

14),15),17) The set of promoters recognized by RNA polymerase holoenzyme is determined by the species of associated < factor.

Prokaryotic genome regulation: a revolutionary paradigm

Although, the mechanism by which the [alpha]-subunit regulates amounts of the holoenzyme is currently unknown, it would be in conjunction with changes in the rate of collagen synthesis.

Cloning and expression analysis of the [alpha]-subunit of porcine prolyl 4-hydroxylase *

During preincubation the apoenzyme and hematin form the active holoenzyme.

Prostaglandin-H-synthase (PGHS)-1 and -2 microtiter assays for the testing of herbal drugs and in vitro inhibition of PGHS-isoenzyms by polyunsaturated fatty acids from Platycodi radix

However, the binding activity of cAMP to the holoenzyme was not inhibited with SGL-II.

A group of glycosphingolipids found in an invertebrate: their structures and biological significance

coli K12 strain (AVB100) containing a chromosomal copy of the biotin holoenzyme synthetase (birA) gene under the control of an L-arabinose-inducible promoter (Avidity Inc.

Use of an in vivo biotinylated single-chain antibody as capture reagent in an immunometric assay to decrease the incidence of interference from heterophilic antibodies

Of equal interest is that, if one coats Protein A Sepharose (PAS) beads with a specific monoclonal antibody to the Ku protein, Ku 162, and then uses these beads to isolate the Ku proteins from the cytoplasmic extracts of fertilized eggs, the beads bind the holoenzyme, and in this bound form the enzyme is active in the absence of (ds)DNA.

Microinjection of an Antibody to the Ku Protein Arrests Development in Sea Urchin Embryos

Koleske have evidence that, in yeast, several SRB proteins chair a committee - called a holoenzyme - that includes RNA polymerase and several other substances important for reading the genetic code.

Scientists find transcription by committee

Hydroxylamine is a carbonyl-specific reagent that reversibly dissociates PLP from the holoenzyme.