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. 2001 Oct;67(10):4701–4707. doi: 10.1128/AEM.67.10.4701-4707.2001

TABLE 1.

Molecular properties of the recombinantly expressed basidiomycete PhyA phytases

Phytase Length (aa)a Predicted cleavage siteb between: N-terminal sequencec N-gly sitesd Mr
pI
Calculated SDS-PAGE Calculatede IEF
P. lycii PhyA 439 A29 and Q30 L31PIPAQXTXN 10 44,583 72,000 4.35 3.61 ± 0.01
A. pediades PhyA 453 G19 and G20 F31PPQIQDSXAAY 6 46,781 59,000 5.00 4.15 ± 0.01
4.66 ± 0.01
4.78 ± 0.01
4.86 ± 0.01
Ceriporia sp. PhyA1 442 A19 and T20 S21VPKNTAPXFX 7 45,942 59,000 6.40 7.36 ± 0.01
8.01 ± 0.03
Ceriporia sp. PhyA2 442 A19 and A20 N25IAPKFSIP 8 44,955 54,000 4.64 3.94 ± 0.01
4.00 ± 0.01
4.06 ± 0.01
4.18 ± 0.01
T. pubescens PhyA 443 A19 and V20 S31AXLDVTRDV 9 44,531 62,000 4.40 3.58 ± 0.02
a

Including the signal sequence. aa, amino acids. 

b

Signal peptide cleavage site predicted with the program SignalP, version 1.1 (17). 

c

Determined from the purified recombinantly expressed phytases. The subscript number indicates the position of the first amino acid determined by Edman sequencing. 

d

Number of potential N-glycosylation (N-gly) sites. 

e

Calculated by using amino acid sequence of the mature protein (i.e., without signal sequence).