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synthase

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synthase

 [sin´thās]
any enzyme, especially a lyase, which catalyzes a synthesis that does not involve the breakdown of a pyrophosphate bond, as opposed to ligase.
Miller-Keane Encyclopedia and Dictionary of Medicine, Nursing, and Allied Health, Seventh Edition. © 2003 by Saunders, an imprint of Elsevier, Inc. All rights reserved.

syn·thase

(sin'thās),
Trivial name used in the Enzyme Commission Report for a lyase reaction going in the reverse direction (NTP-independent). For individual synthases, see the specific names.
See also: synthetase.
Farlex Partner Medical Dictionary © Farlex 2012

synthase

(sĭn′thās′, -thāz′)
The American Heritage® Medical Dictionary Copyright © 2007, 2004 by Houghton Mifflin Company. Published by Houghton Mifflin Company. All rights reserved.

syn·thase

(sin'thās)
Trivial name used in Enzyme Commission Report for a lyase reaction going in the reverse direction (NTP-independent).
See also: synthetase
Medical Dictionary for the Health Professions and Nursing © Farlex 2012
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References in periodicals archive
The transcripts of some nuclear-encoded proteins from the mitochondrial respiratory chain of the shrimp Litopenaeus vannamei are known to be downregulated by hypoxia, including some proteins that compose the Frcatalytic domain of the ATP synthase (Martinez-Cruz et al.
Crystallographic and single-molecule investigations have promoted general understanding of the rotational catalysis mechanism of [F.sub.o][F.sub.1] ATP synthase. However, dynamic mechanism at atomic resolution is not yet well established.
Considering the biological function, we selected two increased proteins: ATP synthase subunit beta (encoding by ATP5B) and complex I subunit (encoding by NDUFS1).
Moreover, these effects were accompanied by significantly decreased PGC-1a protein, mtDNA, ATP synthase, and ND1 at day 14 in the WT/UUO group compared with the WT/Sham group (all P < 0.05; Figures 7 and 8).
Expression of ATP synthase, necessary in the process of oxidative phosphorylation, was found to have decreased.
This pyrene-based sensor was used in HeLa cells to monitor the decrease in ATP levels upon addition of the ATP synthase inhibitor, oligomycin, and upon hydrolysis of ATP to ADP by apyrase (Pak et al., 2015).
From water insoluble fraction, vimentin, gelsolin, gamma enolase like protein, filensin like protein and ATP synthase subunit B were identified.
Human neuronal coenzyme Q10 deficiency results in global loss of mitochondrial respiratory chain activity, increased mitochondrial oxidative stress and reversal of ATP synthase activity: implications for pathogenesis and treatment.
The mitochondria, using the enzyme ATP synthase, use the energy produced in the electron transport chain to manufacture adenosine triphosphate (ATP) from adenosine diphosphate (ADP).
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