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. Author manuscript; available in PMC: 2023 Dec 1.
Published in final edited form as: Trends Parasitol. 2022 Sep 28;38(12):1080–1088. doi: 10.1016/j.pt.2022.09.001

Table 1.

Comparative biochemical characteristics of the four tegumental ectoenzymes that are known to control the S. mansoni purinergic halo.

SmATPDase1 SmNPP5 SmNACE SmAP
Size (AA#) 544 458 303 536
Mol Mass (Da) 61,353 52,563 34,758 59,375
pI 9.11 6.28 7.13 5.92
GPI-linked + + +
Glycoprotein ? + + +
pH optimum (range) ATP: 8.5–10
ADP: 7.5–10
ATP: 8–8.5
ADP: 7–10
ATP: 7–8
ADP: 7–10
ATP: 9
ADP: 8–10
Cation requirement Ca≥Mg Mg=Ca=Zn None Mg >>Ca>Zn>Cu
Substrates (K m , μM±SD) ATP (400 ±20)
ADP (252 ±20)
NAD (200 ±0.6)
ATP (217 ±26)
ADP (246 ±34)
ADPR
NAD (49 ±3.5)
NADP (14 ±2.9)
NDG (23 ±1.1)
NMN (1084 ±164)
AMP (650 ±22)
CMP (630 ±20)
GMP (640 ±11)
TMP (595 ±33)
pNPP (288 ±12)
polyP (6900 ±1000)
S1P, PLP
Accession# AY323529 EU769293 AAX35328 EU040139
References [23, 24] [25, 2628, 40] [35, 40, 45] [29, 30, 53, 56, 57]

Km values reported here were measured at each enzyme’s optimal pH. Whether SmATPDase1 is glycosylated is unknown, indicated by “?”. GenBank accession numbers for each enzyme are listed. AA#: amino acid number, Mol Mass (Da): Molecular Mass (Daltons), pI: isoelectric point. The full designations of most listed substrates are given in Figure 1. NADP, nicotinamide adenine dinucleotide phosphate; NGD, nicotinamide guanine dinucleotide; pNPP p-nitrophenyl phosphate; polyP, polyphosphate; S1P, sphingosine-1-phosphate; PLP, pyridoxal phosphate.