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. Author manuscript; available in PMC: 2010 Jul 14.
Published in final edited form as: Biochemistry. 2009 Jul 14;48(27):6469–6481. doi: 10.1021/bi900661b

Table 4.

Kinetic parameters for Gox1177 with selected substratesa

Compound kcat, s−1 Km, mM kcat/Km, M−1s−1
N-acetyl-d-Ala 50 ± 4 18 ± 2 (2.9 ± 0.4) × 103
N-acetyl-d-Val 16 ± 1 4.1 ± 0.2 (3.9 ± 0.2) × 103
N-acetyl-d-Leu 101 ± 3 3.2 ± 0.2 (3.2 ± 0.2) × 104
N-acetyl-d-Met 40 ± 2 1.8 ± 0.3 (2.2 ± 0.4) × 104
N-acetyl-d-His nd nd (8.5 ± 0.2) × 103
N-acetyl-d-Trp 89 ± 2 2.2 ± 0.2 (4.1 ± 0.3) × 104
N-acetyl-d-Phe 59 ± 2 2.5 ± 0.3 (2.4 ± 0.3) × 104
N-acetyl-d-Tyr 66 ± 2 7.1 ± 0.5 (9.3 ± 0.7) × 103
N-acetyl-d-Thr nd nd (6.0 ± 0.1) × 103
N-acetyl-d-Asn nd nd 480 ± 20
N-acetyl-d-Gln nd nd (2.7 ± 0.1) × 103
N-formyl-d-Leu 13 ± 1 5.9 ± 0.5 (2.2 ± 0.2) × 103
N-succinyl-d-Leu nd nd 30 ± 1.4
N-propionyl-d-Leu 23 ± 1 1.2 ± 0.1 (2.0 ± 0.1) × 104
l-Leu-d-Leu 31 ± 1 3.3 ± 0.2 (9.2 ± 0.7) × 103
l-Met-d-Leu 20 ± 1 1.6 ± 0.2 (1.3 ± 0.2) × 104
l-Tyr-d-Leu 19 ± 1 1.3 ± 0.2 (1.5 ± 0.2) × 104
a

From fits of the data to equation 2.