. 2009 Mar 20;66(13):2075–2091. doi: 10.1007/s00018-009-0007-5

Table 1.

Kinetic parameters for the cleavage of OT/Np-related peptides adopting β-turn, β-sheet, or α-helix conformations [46]

Peptides	Amino acid sequences																					K _m (μM)	V _max (pmol/h)
	1						7									15					20
							P	L	G	G	K	R	↓	A	V	L						150	720
[S ⁷ –G ¹⁰]OT/Np(7–15)							S	S	N	G	K	R	↓	A	V	L						350	990
[Y ⁷ –G ¹⁰]OT/Np(7–15)							Y	K	G	G	K	R	↓	A	V	L						370	2,810
[N ⁷ –A ¹⁰]OT/Np(7–15)							N	N	I	A	K	R	↓	A	V	L						430	1,420
OT/Np(7–15)							P	L	G	G	K	R	↓	A	V	L						150	720
[I ⁷ –L ¹⁰]OT/Np(7–15)							I	A	V	L	K	R	↓	A	V	L						6,450	4,730
OT/Np(7–20)							P	L	G	G	K	R	↓	A	V	L	D	L	D	V	R	140	550
[I ⁷ –L ¹⁰]OT/Np(7–20)							I	A	V	L	K	R	↓	A	V	L	D	L	D	V	R	2,880	4,280
OT/Np(1–20)	C	Y	I	Q	N	C	P	L	G	G	K	R	↓	A	V	L	D	L	D	V	R	100	260
[A ³ –V ¹⁰]OT/Np(3–20)			A	V	L	D	D	L	D	V	K	R	↓	A	V	L	D	L	D	V	R	4,760	480

The bold values correspond to values obtained for the peptides in which a sequence or a residue was modified or deleted

↓ Arrows indicate cleavage of substrates