DOQCS Database

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	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	3.8	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

Enzyme List