“Peptide deformylase”的意思、由来-开放百科全书

词条

Peptide deformylase

释义

Structural studies
References

{{enzyme
| Name = peptide deformylase
| EC_number = 3.5.1.88
| CAS_number =
| IUBMB_EC_number = 3/5/1/88
| GO_code = 0042586
| image =
| width =
| caption =
}}

In enzymology, a peptide deformylase ({{EC number|3.5.1.88}}) is an enzyme that catalyzes the chemical reaction

formyl-L-methionyl peptide + H₂O formate + methionyl peptide

Thus, the two substrates of this enzyme are formyl-L-methionyl peptide and H₂O, whereas its two products are formate and methionyl peptide.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is formyl-L-methionyl peptide amidohydrolase.

Structural studies

As of late 2007, 34 structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|1IX1}}, {{PDB link|1LM4}}, {{PDB link|1LM6}}, {{PDB link|1LME}}, {{PDB link|1LQW}}, {{PDB link|1LQY}}, {{PDB link|1LRU}}, {{PDB link|1LRY}}, {{PDB link|1N5N}}, {{PDB link|1Q1Y}}, {{PDB link|1S17}}, {{PDB link|1SV2}}, {{PDB link|1SZZ}}, {{PDB link|1V3Y}}, {{PDB link|1VEV}}, {{PDB link|1VEY}}, {{PDB link|1VEZ}}, {{PDB link|1WS0}}, {{PDB link|1WS1}}, {{PDB link|1XEM}}, {{PDB link|1XEN}}, {{PDB link|1XEO}}, {{PDB link|1Y6H}}, {{PDB link|1ZXZ}}, {{PDB link|1ZY0}}, {{PDB link|1ZY1}}, {{PDB link|2AI7}}, {{PDB link|2AI8}}, {{PDB link|2AI9}}, {{PDB link|2AIA}}, {{PDB link|2AIE}}, {{PDB link|2EW5}}, {{PDB link|2EW6}}, and {{PDB link|2EW7}}.

References

{{cite journal | author = Adams JM | year = 1968 | title = On the release of the formyl group from nascent protein | journal = J. Mol. Biol. | volume = 33 | pages = 571–89 | pmid = 4973445 | doi = 10.1016/0022-2836(68)90307-0 | issue = 3 }}
{{cite journal |vauthors=Mazel D, Pochet S, Marliere P | year = 1994 | title = Genetic characterization of polypeptide deformylase, a distinctive enzyme of eubacterial translation | journal = EMBO J. | volume = 13 | pages = 914–23 | pmid = 8112305 | issue = 4 | pmc = 394892 }}
{{cite journal |vauthors=Chan MK, Gong W, Rajagopalan PT, Hao B, Tsai CM, Pei D | year = 1997 | title = Crystal structure of the Escherichia coli peptide deformylase | journal = Biochemistry | volume = 36 | pages = 13904–9 | pmid = 9374869 | doi = 10.1021/bi9711543 | issue = 45 }}
{{cite journal |vauthors=Becker A, Schlichting I, Kabsch W, Schultz S, Wagner AF | year = 1998 | title = Structure of peptide deformylase and identification of the substrate binding site | journal = J. Biol. Chem. | volume = 273 | pages = 11413–6 | pmid = 9565550 | doi = 10.1074/jbc.273.19.11413 | issue = 19 }}
{{cite journal |vauthors=Becker A, Schlichting I, Kabsch W, Groche D, Schultz S, Wagner AF | year = 1998 | title = Iron center, substrate recognition and mechanism of peptide deformylase | journal = Nat. Struct. Biol. | volume = 5 | pages = 1053–8 | pmid = 9846875 | doi = 10.1038/4162 | issue = 12 }}
{{cite journal | vauthors = Rajagopalan PT, Yu XC, Pei D | year = 1997 | title = Peptide deformylase: a new type of mononuclear iron protein | journal = J. Am. Chem. Soc. | volume = 119 | pages = 12418–12419 | doi = 10.1021/ja9734096 | issue = 50 }}
{{cite journal |vauthors=Groche D, Becker A, Schlichting I, Kabsch W, Schultz S, Wagner AF | year = 1998 | title = Isolation and crystallization of functionally competent Escherichia coli peptide deformylase forms containing either iron or nickel in the active site | journal = Biochem. Biophys. Res. Commun. | volume = 246 | pages = 342–6 | pmid = 9610360 | doi = 10.1006/bbrc.1998.8616 | issue = 2 }}
{{cite journal |vauthors=Rajagopalan PT, Grimme S, Pei D | year = 2000 | title = Characterization of cobalt(II)-substituted peptide deformylase: function of the metal ion and the catalytic residue Glu-133 | journal = Biochemistry | volume = 39 | pages = 779–90 | pmid = 10651644 | doi = 10.1021/bi9919899 | issue = 4 }}
{{cite journal |vauthors=Hu YJ, Wei Y, Zhou Y, Rajagopalan PT, Pei D | year = 1999 | title = Determination of substrate specificity for peptide deformylase through the screening of a combinatorial peptide library | journal = Biochemistry | volume = 38 | pages = 643–50 | pmid = 9888804 | doi = 10.1021/bi9820412 | issue = 2 }}
{{cite journal |vauthors=Ragusa S, Mouchet P, Lazennec C, Dive V, Meinnel T | year = 1999 | title = Substrate recognition and selectivity of peptide deformylase Similarities and differences with metzincins and thermolysin | journal = J. Mol. Biol. | volume = 289 | pages = 1445–57 | pmid = 10373378 | doi = 10.1006/jmbi.1999.2832 | issue = 5 }}
{{cite journal |vauthors=Giglione C, Pierre M, Meinnel T | year = 2000 | title = Peptide deformylase as a target for new generation, broad spectrum antimicrobial agents | journal = Mol. Microbiol. | volume = 36 | pages = 1197–205 | pmid = 10931273 | doi = 10.1046/j.1365-2958.2000.01908.x | issue = 6 }}
{{cite journal | author = Pei D | year = 2001 | title = Peptide deformylase: a target for novel antibiotics? | journal = Emerging Therapeutic Targets | volume = 5 | pages = 23–40 | doi = 10.1517/14728222.5.1.23 | pmid = 15992166 | issue = 1 }}

{{Carbon-nitrogen non-peptide hydrolases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}{{3.5-enzyme-stub}}

2 : EC 3.5.1|Enzymes of known structure

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