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. 2013 Feb 4;110(8):E653–E661. doi: 10.1073/pnas.1221050110

Table 1.

Active site parameters of convergently related Ser proteases

Clan Enzyme PDB Complex Reactive rotamer ϕ, ψ angles Catalytic motif Oxyanion hole Face of attack χcat αcat χoxy Reference
PA Elastase 3HGN Hemiketal g− (−43, 140) S-H-D N re −131 125 −32 (68)
SB Sedolisin 1GA4 Ester g− (−62, −24) S-E-D N re −147 108 −18 (69)
SE D-Ala-D-Ala peptidase 1MPL Phophonate g− (−72, 0) S-Y-K N re −156 97 −48 (70)
SC Prolyl aminopeptidase 1QFM Hemiketal t (66, −115) S-H-D N + 1 si 117 106 32 (26)
SS L,D-carboxypeptidase 1ZRS t (64, −130) S-H-E N + 1 si 109 (49)
PC Aspartyl dipeptidase 1FYE t (57, −122) S-H-E N + 1 si 84 (71)
SH CMV protease 1NKM α-Ketoamide t (−177, 132) S-H-H Extrinsic re −125 111 −39 (23)
SK ClpP 1FZS HMK t (59, −122) S-H-D N + 1 si 130 74 50 (29)
SF Signal peptidase 1B12 Ester g+ (−68, −11) S-K N si 148 109 1 (60)
SJ VP4 protease 3R0B Ester g+ (−65, −13) S-K N si 173 114 −9 (72)
ST Rhomboid-1 2IC8 g+ (−63, −29) S-H N si 113 (73)

Halomethyl ketone (HMK) inactivators give rise to unusually small αcat values. See text for details.