Table 3.
Recognition sequences for the modification of the active site cysteine to FGly in enzymes expressed in E. coli, and the percentage of FGly transformation.
| Type I sulfatase | Sequence | FGly presence | Method for FGly determination | Enzyme co-expressed | Ref. |
|---|---|---|---|---|---|
| F. heparinum | (69)GTRFTRAYCAQPLCTPSRSAIFSG | 100% | MALDI-MS | [39] | |
| FH2S | |||||
| C. perfringens | (37)GYNFENAYTAVPSCIASRASILTG | Partially | MALDI-TOF | – | [40] |
| (BAB79937.1) | 100% | anSME | |||
| P. aeruginosa | (39)GLRLTDFHTAST-CSPTRSMLLTG | 95% | DTNB | – | [41] |
| (CAA88421.2) | |||||
| E. meliloti | (41)SARFHNNYTSSPLCAPARASFMAG | 0% | DTNB | – | This work |
| (AAC13371.1) | |||||
| M. tuberculosis | (45)GILFTRAHATAPLCTPSRGSLFTG | NDa | – | – | [38] |
| (F70837) | |||||
| H. sapiens | (66)GLLFPNFYSANPLCSPSRAALLTG | NDa | – | – | [42] |
| (NP_000503.1) | |||||
| H. sapiens | (71)SLLFQNAFAQQAVCAPSRVSFLTG | NDa | – | – | [43] |
| (AAC77828.1) | |||||
| P. sp ATCC19151 (CBI83290.1) | (40)GVVFDSAYCNSPLCAPSRFTLVSG | ND | – | – | [23] |
| F. heparinum | (67)GMLFNNCFVTNAVCGPSRATILTG | ND | – | – | [44] |
| FH6S | |||||
| F. heparinum | (67)GVRFTNAFCSSPSCTPARAGMLTG | ND | – | – | [45] |
| NSulf | |||||
| H. pomatia | (71)GVRLENYYVQ-PICTPTRSQLMSG | b | – | – | [46] |
| (AAF30402.1) | |||||
| Phosphonate monoester hydrolase | |||||
| R.leguminosarum | (49)GTLFRRHYAGAAPCSPARATLYTG | 25% | Fluorophore labeling | – | [47] |
| (WP025417352.1) | 62% | MtbFGE | |||
| B. caryophylli | (45)GLTFRNHVTTCVPCGPARASLLTG | Partially | MALDI-TOF | – | [48] |
| (AAC44467.1) | Partiallyc | MtbFGE | |||
ND: Not determined.
a
Low activity suggest none or poor FGly modification.
b
Expression in E. coli was not successful.
c
Partially, but greater than without MtbFGE.