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Enzyme List for pathway sGC (Pathway Number 140) | | Molecule Name/
Site Name | Km (uM) | kcat (1/s) | Ratio
(k2/k3) | Enzyme Type | Substrate | Product |
| 1 |
Enzyme Activity:
activeGC
Enzyme Molecule:
GC5_CO | 0.5 | 54.54 | 4 | Classical Michaelis-Menten
V = Etot.S.Kcat/Km+S | GTP
| cGMP
| | | Friebe et al., 1996, EMBO Journal, 15(24): 6863-6868 and back refs cited in their paper. They have studied the potentiation by YC-1 of CO activated sGC. In the absence of YC-1, they report 3 fold stimulation of GC by CO, with 218 +- 11 nmol/min/mg of cGMP. Vmax / Km increased by 100 X. |
| 2 |
Enzyme Activity:
HOXY
Enzyme Molecule:
Hemeoxyg2 | 3.80004 | 0.3556 | 4 | explicit E-S complex | Heme
| CO
| | | Ingi et al., J Neurosci., 1996, 16(18):5621-5628, report the production rates of heme precursors and metabolites. The rate reported for CO from heme is 2.9 pmol/mg protein over 6 hr. Their results indicate high HO activity in brain (along with significant levels of heme) at around 280pmol of bilirubin/mg/min. Montellano PRO, Curr. Opin. in Chem. Biol, 2000,4:221-227 and refs cited in his paper were also studied initially. Km for free heme is around 3.8 +/- 0.5 uM.(Bonkovsky et al., 1990, 189(1):155-166) |
| 3 |
Enzyme Activity:
kenz
Enzyme Molecule:
PDE | 2 | 3.87 | 4 | explicit E-S complex | cGMP
| 5prime_GMP
| | | Km / Vmax -- 2 uM / 3.87 sec^-1. rates from Turko et al., 1998, Biochem J, 329:505-510 and Kuroda et al., J Neurosci, 2001, 21(15):5693-5702 |
Pathway Details Molecule List Enzyme List Reaction List
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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