| Name | Pro 1 |
|---|---|
| Synonyms | HGPS; PRO 1; PRO1; progeria 1 (Hutchinson Gilford type); progeria 1 (Hutchinson Gilford type)s |
| Name | 1,3-dichloropropene |
|---|---|
| CAS | 1,3-dichloro-1-propene |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 15571384 | Poelarends GJ, Serrano H, Johnson WH Jr, Hoffman DW, Whitman CP: The hydratase activity of decarboxylase: mechanistic and evolutionary implications. J Am Chem Soc. 2004 Dec 8;126(48):15658-9. Both the hydratase activity and the pKa value of Pro-1 are shared with trans-3-chloroacrylic acid dehalogenase, another tautomerase superfamily member that precedes MSAD in a bacterial degradation pathway for trans-1,3-dichloropropene. |
33(0,1,1,3) | Details |
| 15982004 | Poelarends GJ, Serrano H, Johnson WH Jr, Whitman CP: Inactivation of decarboxylase by 3-halopropiolates: evidence for hydratase activity. Biochemistry. 2005 Jul 5;44(26):9375-81. The results provide additional evidence for the hydratase activity of MSAD and further support for the hypothesis that MSAD and trans-3-chloroacrylic acid dehalogenase, the preceding enzyme in the trans-1,3-dichloropropene catabolic pathway, diverged from a common ancestor but conserved the necessary catalytic machinery for the conjugate addition of water. Sequence analysis, chemical labeling studies, site-directed mutagenesis, and NMR studies of MSAD identified Pro-1 as a key active site residue in which the amino group has a pKa value of 9.2. |
3(0,0,0,3) | Details |
| 17121835 | de Jong RM, Bazzacco P, Poelarends GJ, Johnson WH Jr, Kim YJ, Burks EA, Serrano H, Thunnissen AM, Whitman CP, Dijkstra BW: Crystal structures of native and inactivated cis-3-chloroacrylic acid dehalogenase. J Biol Chem. 2007 Jan 26;282(4):2440-9. Epub 2006 Nov 22. The bacterial degradation pathways for the nematocide 1,3-dichloropropene rely on hydrolytic dehalogenation reactions catalyzed by cis- and trans-3-chloroacrylic acid dehalogenases (cis-CaaD and CaaD, respectively). They locate four known catalytic residues (Pro-1, Arg-70, Arg-73, and -114) and two previously unknown, potential catalytic residues (His-28 and Tyr-103'). |
3(0,0,0,3) | Details |
| 16274229 | Almrud JJ, Poelarends GJ, Johnson WH Jr, Serrano H, Hackert ML, Whitman CP: Crystal structures of the wild-type, P1A mutant, and inactivated decarboxylase: a structural basis for the decarboxylase and hydratase activities. Biochemistry. 2005 Nov 15;44(45):14818-27. decarboxylase (MSAD) from Pseudomonas pavonaceae 170 is a tautomerase superfamily member that converts to by a mechanism utilizing Pro-1 and Arg-75. The results also provide additional evidence supporting the hypothesis that MSAD and trans-3-chloroacrylic acid dehalogenase, a tautomerase superfamily member preceding MSAD in the trans-1,3-dichloropropene degradation pathway, diverged from a common ancestor but retained the key elements for the conjugate addition of water. |
3(0,0,0,3) | Details |
| 11418568 | Poelarends GJ, Saunier R, Janssen DB: trans-3-Chloroacrylic acid dehalogenase from Pseudomonas pavonaceae 170 shares structural and mechanistic similarities with 4-oxalocrotonate tautomerase. J Bacteriol. 2001 Jul;183(14):4269-77. The genes (caaD1 and caaD2) encoding the trans-3-chloroacrylic acid dehalogenase (CaaD) of the 1,3-dichloropropene-utilizing bacterium Pseudomonas pavonaceae 170 were cloned and heterologously expressed in Escherichia coli and Pseudomonas sp. strain GJ1. The sequence conservation between CaaD and 4-OT and site-directed mutagenesis experiments suggested that Pro-1 of the beta-subunit and Arg-11 of the alpha-subunit are active-site residues in CaaD. |
2(0,0,0,2) | Details |
| 14701869 | de Jong RM, Brugman W, Poelarends GJ, Whitman CP, Dijkstra BW: The X-ray structure of trans-3-chloroacrylic acid dehalogenase reveals a novel hydration mechanism in the tautomerase superfamily. J Biol Chem. 2004 Mar 19;279(12):11546-52. Epub 2003 Dec 29. Isomer-specific 3-chloroacrylic acid dehalogenases function in the bacterial degradation of 1,3-dichloropropene, a compound used in agriculture to kill plant-parasitic nematodes. The crystal structure of the heterohexameric trans-3-chloroacrylic acid dehalogenase (CaaD) from Pseudomonas pavonaceae 170 inactivated by 3-bromopropiolate shows that -52 in the alpha-subunit is positioned to function as the water-activating base for the addition of a group to C-3 of 3-chloroacrylate and 3-bromopropiolate, whereas the nearby Pro-1 in the beta-subunit is positioned to provide a to C-2. |
2(0,0,0,2) | Details |
| 19856961 | Robertson BA, Schroeder GK, Jin Z, Johnson KA, Whitman CP: Pre-steady-state kinetic analysis of cis-3-chloroacrylic acid dehalogenase: analysis and implications. Biochemistry. 2009 Dec 15;48(49):11737-44. A comparison of the unliganded cis-CaaD crystal structure with that of an inactivated cis-CaaD where the prolyl of Pro-1 is covalently attached to (R)- provides a possible explanation for the isomerization step. These reactions represent key steps in the degradation of the nematocide, 1,3-dichloropropene. |
1(0,0,0,1) | Details |
| 15381403 | Poelarends GJ, Whitman CP: Evolution of enzymatic activity in the tautomerase superfamily: mechanistic and structural studies of the 1,3-dichloropropene catabolic enzymes. Bioorg Chem. 2004 Oct;32(5):376-92. These are the first structural and mechanistic details for tautomerase superfamily members that catalyze either a hydration or a decarboxylation reaction, rather than a tautomerization reaction, in which Pro-1 serves as a general acid catalyst rather than as a general base catalyst. |
1(0,0,0,1) | Details |
| 17661448 | Poelarends GJ, Johnson WH Jr, Serrano H, Whitman CP: Phenylpyruvate tautomerase activity of trans-3-chloroacrylic acid dehalogenase: evidence for an enol intermediate in the dehalogenase reaction?. Biochemistry. 2007 Aug 21;46(33):9596-604. Epub 2007 Jul 28. The enzymatic conversion of cis- or trans-3-chloroacrylic acid to is a key step in the bacterial degradation of the nematocide 1,3-dichloropropene. CaaD and cis-CaaD represent different families in the tautomerase superfamily, a group of structurally homologous proteins characterized by a core beta-alpha-beta building block and a catalytic Pro-1. |
1(0,0,0,1) | Details |
| 12873137 | Wang SC, Person MD, Johnson WH Jr, Whitman CP: Reactions of trans-3-chloroacrylic acid dehalogenase with acetylene substrates: consequences of and evidence for a hydration reaction. Biochemistry. 2003 Jul 29;42(29):8762-73. The inactivation observed for 3-bromopropiolic acid is due to the covalent modification of Pro-1 of the beta-subunit. Various soil bacteria use 1,3-dichloropropene, a component of the commercially available fumigants Shell D-D and Telone II, as a sole source of carbon and energy. |
1(0,0,0,1) | Details |
| 16784221 | Poelarends GJ, Almrud JJ, Serrano H, Darty JE, Johnson WH Jr, Hackert ML, Whitman CP: Evolution of enzymatic activity in the tautomerase superfamily: mechanistic and structural consequences of the L8R mutation in 4-oxalocrotonate tautomerase. Biochemistry. 2006 Jun 27;45(25):7700-8. CaaD, from Pseudomonas pavonaceae 170, catalyzes the hydrolytic dehalogenation of trans-3-chloroacrylate in the trans-1,3-dichloropropene degradation pathway. |
0(0,0,0,0) | Details |