. 2011 Mar 22;42(5):1757–1764. doi: 10.1007/s00726-011-0890-6

Table 1.

Isomerization rate of different substrates relative to the amino-terminal sequence of bombinin H. Rates with different amino acids at position 2 (A), 1 (B) and 3 (C) are shown. D: Mammalian peptides tested

		Reaction rates		Equilibrium constant
		Absolute (μM h⁻¹)	Relative (%)	Equilibrium constant
(A)	IIGPVLĊa	110	100	1.1
	Fg	1,220	1,100	0.59
	M	1,170	1,100	1.44
	F	1,060	1,000	2.85
	Nl	1,000	900	1.33
	L	240	222
	W	135	130	1.86
	Ċ	78	70	0.66
	A	24	22
	D	19°	17	1.32
	K	13°	12	1.28
	Q	10°	9	0.7
	T	9	8	0.66
	E	<4°	<3°
(B)	IIGPVLĊa	110	100
	F	187	170
	W	140	130
	E	6.5	4
	Y	1.5	1
	A	<0.4	<1
	KIA	2.5	<3
	SIA	N.d.	–
	GIA	N.d.	–
(C)	IIGPVLĊa	110	100
	F	8	3.5
	A	7	3.3
	D	0.1	<0.2
	K	N.d.	–
	Q	N.d.	–
	IFF	116	107
	IĊF	5	1.2
(D)	IIGPVLĊa	++
	IMFFEMĊa^a	+++
	LLGDFFĊa^b	++
	FVNQHLa^c	+
	FLFQPQRFa^d	+++

Fg phenylglycine, Nl norleucine, Ċ Cys with Bodipy attached via thioether linkage; n.d. not detectable (below 0.05 μM h⁻¹)

^a DLP-2/4(1–6)

^b LL-37(1–6)

^c Insulin B-chain (1–6)

^d Neuropeptide FF (full length)

° Uncorrected reaction rates