![]() GUANOSINE 5'-TETRAPHOSPHATE TRIS SALT structure
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Common Name | GUANOSINE 5'-TETRAPHOSPHATE TRIS SALT | ||
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CAS Number | 103213-27-0 | Molecular Weight | 724.29500 | |
Density | N/A | Boiling Point | N/A | |
Molecular Formula | C14H28N6O20P4 | Melting Point | N/A | |
MSDS | USA | Flash Point | N/A | |
Symbol |
![]() GHS08 |
Signal Word | Warning |
Polyphosphatase activity of CthTTM, a bacterial triphosphate tunnel metalloenzyme.
J. Biol. Chem. 283 , 31047-31057, (2008) Triphosphate tunnel metalloenzymes (TTMs) are a superfamily of phosphotransferases with a distinctive active site located within an eight-stranded beta barrel. The best understood family members are the eukaryal RNA triphosphatases, which catalyze the initial... |
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Structural requirements for the activation of Escherichia coli CTP synthase by the allosteric effector GTP are stringent, but requirements for inhibition are lax.
J. Biol. Chem. 283 , 2010-2020, (2008) Cytidine 5'-triphosphate synthase catalyzes the ATP-dependent formation of CTP from UTP using either NH(3) or l-glutamine (Gln) as the source of nitrogen. GTP acts as an allosteric effector promoting Gln hydrolysis but inhibiting Gln-dependent CTP formation a... |
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Overexpression of a Zn2+-sensitive soluble exopolyphosphatase from Trypanosoma cruzi depletes polyphosphate and affects osmoregulation.
J. Biol. Chem. 282 , 32501-32510, (2007) We report the cloning, expression, purification, and characterization of the Trypanosoma cruzi exopolyphosphatase (TcPPX). The product of this gene (TcPPX), has 383 amino acids and a molecular mass of 43.1 kDa. TcPPX differs from most exopolyphosphatases in i... |
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Inhibitors of guanylate cyclase inhibit phototransduction in limulus ventral photoreceptors.
Vis. Neurosci. 18 , 625-632, (2001) The second messenger systems involved in the final stages of the phototransduction cascade in Limulus photoreceptors remain unclear. Excised patches of transducing membrane contain cGMP-gated channels, suggesting the involvement of cGMP in the excitation proc... |
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Adenosine-5'-tetraphosphate and guanosine-5'-tetraphosphate: new substrates of the cytosolic exopolyphosphatase of the yeast Saccharomyces cerevisiae.
Biochemistry. (Mosc.) 62 , 1051-1052, (1997) A cytosolic preparation of Saccharomyces cerevisiae is capable of hydrolyzing adenosine-5'-tetraphosphate and guanosine-5'-tetraphosphate with activities which are 1.5-2 times greater than that with polyP15. The apparent K(m) values for hydrolysis of adenosin... |
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