Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015 (Sat)
Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015 (Sat)
Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015 (Sat)
Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015 (Sat)
Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015 (Sat)

Escherichia coli K-12 substr. MG1655 Enzyme: FKBP-type peptidyl prolyl cis-trans isomerase

Gene: slyD Accession Numbers: EG11663 (EcoCyc), b3349, ECK3336

Synonyms: WHP

Regulation Summary Diagram: ?

Regulation summary diagram for slyD

Subunit composition of FKBP-type peptidyl prolyl cis-trans isomerase = [SlyD]2
         FKBP-type peptidyl prolyl cis-trans isomerase = SlyD

SlyD is a peptidyl prolyl cis/trans-isomerase (PPIase) and chaperone. The protein has a C-terminal metal binding domain and binds Zn2+ and Ni2+ ions [Wulfing94] as well as Cu+ and Co2+ in vitro [Kaluarachchi11]. Its PPIase activity is regulated by Ni2+ binding to the histidine-rich C-terminus [Hottenrott97]. Ni2+ binding increases the thermodynamic stability of both SlyD domains [Haupt11]. In vivo under anaerobic conditions, SlyD can specifically influence the balance of nickel ions in the cell [Kaluarachchi11]. SlyD serves as a Ni2+ reservoir for [NiFe]-hydrogenase biosynthesis [Kaluarachchi11a]. The binding of Cu+ and Ni2+ to two C-terminal peptides has been studied [Witkowska12].

A protein consisting of the N-terminal 165 amino acids of SlyD (SlyD*) efficiently catalyzes refolding of reduced and carboxymethylated RNase T1; the enzyme is inhibited by FK506, and kinetics of the refolding activity have been measured [Scholz06]. The "insert-in-flap" (IF) chaperone domain near the prolyl isomerase active site within SlyD* appears to be necessary and sufficient to confer chaperone activity for proline-limited folding [Knappe07]; it recognizes and binds unfolded and partially folded proteins [Weininger09]. After the IF domain forms an initial dynamic complex with unfolded proteins, they are transferred to the prolyl isomerase domain [Zoldak11]. The substrate specificity of SlyD* was measured using a library of fluorescent peptides, showing high activity with hydrophobic residues such as Leu, Tyr, and Phe preceding proline [Zoldak09]. However, in a protein context, activity was not dependent on the amino acid residue before the proline [Jakob09]. SlyD promotes very fast prolyl isomerization in an unfolded protein; in proteins that already contain the correct prolyl isomer, SlyD thus retards conformational folding [Zoldak13].

SlyD is involved in the insertion of Ni2+ during the maturation of hydrogenases. SlyD has been shown to interact directly with HypB, an accessory protein required for hydrogenase maturation [Zhang05c], and transfers Ni2+ to HypB [Kaluarachchi11a]. A loop in the SlyD chaperone domain is required for interaction with HypB, and the interaction is important for hydrogenase maturation. The C-terminal metal-binding domain of SlyB is required for stimulating metal release from HypB and for hydrogenase activation [Leach07], while the PPIase activity is not required for hydrogenase maturation [Zhang07c]. Interaction with SlyD increases the GTPase activity of HypB [Kaluarachchi11a]. SlyD also interacts directly with HycE, the large subunit of hydrogenase 3, via its IF domain [Chung11]. Although a truncated mutant protein, SlyD155, is able to bind a single Ni2+ ion and interacts with HypB, it is unable to activate release of Ni2+ from HypB and does not activate hydrogenase [Kaluarachchi12].

SlyD (as well as DnaK) binds to Tat signal sequences in vivo and in vitro [Graubner07]. SlyD binds ATP, but does not hydrolyze it; binding is enhanced by bivalent transition metal ions, especially Zn2+ and Ni2+ [Mitterauer99].

SlyD is required for phage φX174-induced cell lysis [Roof94]. Its function appears to be in the stabilization of the φX174 lysis protein E [Bernhardt02]. A peptide consisting of the N-terminal transmembrane domain of protein E inhibits the peptidyl prolyl isomerase activity of SlyD [Mendel06].

Gel filtration experiments indicate that SlyD is a dimer in solution [Mitterauer99], while an N-terminal fragment of SlyD (aa 1-165) appears to be monomeric [Scholz06]. A later study indicates that SlyD is monomeric and contains multiple metal binding sites [Kaluarachchi09]. Solution structures of full-length SlyD [Martino09, Martino09a] and SlyD* [Weininger09] have been solved. The FKBP and IF domains do not have a fixed relative location [Weininger09]. An additional C-terminal α-helix is packed against the atypical PPIase domain and appears to be involved in nickel ion binding and conformational rearrangement of the PPIase domain [Martino09]. The kinetics of folding of the SlyD* protein with or without the IF domain (a "guest domain" located in a loop of the FKBP domain) has been studied [Zoldak09a].

Overexpression of slyD is toxic, causing filamentation [Roof94, Roof97]. In the E. coli B and C strains, slyD mutations cause a significant growth rate defect [Roof97].

SlyD: "sensitivity to lysis D" [Maratea85]

Review: [Kovermann13]

Citations: [Mukherjee03, BolanosGarcia06, Kovermann11, Haupt11a, Kovermann13a]

Locations: cytosol

Map Position: [3,475,929 <- 3,476,519] (74.92 centisomes, 270°)
Length: 591 bp / 196 aa

Molecular Weight of Polypeptide: 20.853 kD (from nucleotide sequence)

Molecular Weight of Multimer: 44 kD (experimental) [Mitterauer99]

Unification Links: ASAP:ABE-0010946 , CGSC:35441 , DIP:DIP-31853N , EchoBASE:EB1614 , EcoGene:EG11663 , EcoliWiki:b3349 , Mint:MINT-1223693 , ModBase:P0A9K9 , OU-Microarray:b3349 , PortEco:slyD , PR:PRO_000023959 , Pride:P0A9K9 , Protein Model Portal:P0A9K9 , RefSeq:NP_417808 , RegulonDB:EG11663 , SMR:P0A9K9 , String:511145.b3349 , UniProt:P0A9K9

Relationship Links: InterPro:IN-FAMILY:IPR001179 , InterPro:IN-FAMILY:IPR023566 , Panther:IN-FAMILY:PTHR10516 , PDB:Structure:2K8I , PDB:Structure:2KFW , Pfam:IN-FAMILY:PF00254 , Prosite:IN-FAMILY:PS50059

In Paralogous Gene Group: 8 (2 members)

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0009408 - response to heat Inferred from experiment [Han07a]
GO:0022417 - protein maturation by protein folding Inferred from experiment [Zhang05c]
GO:0042026 - protein refolding Inferred from experiment [Scholz06]
GO:0050821 - protein stabilization Inferred from experiment [Han07a]
GO:0051604 - protein maturation Inferred from experiment [Leach07]
GO:0000413 - protein peptidyl-prolyl isomerization Inferred by computational analysis [Gaudet10]
GO:0006457 - protein folding Inferred by computational analysis [GOA01]
GO:0061077 - chaperone-mediated protein folding Inferred by computational analysis [Gaudet10]
Molecular Function: GO:0003755 - peptidyl-prolyl cis-trans isomerase activity Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01a, Zhang07c, Hottenrott97]
GO:0005507 - copper ion binding Inferred from experiment [Kaluarachchi11]
GO:0005515 - protein binding Inferred from experiment [Chan11, Butland05, Chung11, Zhang05c, Butland06]
GO:0008270 - zinc ion binding Inferred from experiment [Kaluarachchi11, Wulfing94]
GO:0016151 - nickel cation binding Inferred from experiment [Kaluarachchi11, Kaluarachchi09, Wulfing94, Martino09]
GO:0050897 - cobalt ion binding Inferred from experiment [Kaluarachchi11]
GO:0051082 - unfolded protein binding Inferred from experiment [Weininger09]
GO:0005528 - FK506 binding Inferred by computational analysis [Gaudet10]
GO:0016853 - isomerase activity Inferred by computational analysis [UniProtGOA11]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, Gaudet10]

MultiFun Terms: information transfer protein related chaperoning, repair (refolding)

Essentiality data for slyD knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 1]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 2]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 1]

Created 16-Apr-2007 by Keseler I , SRI International
Last-Curated ? 08-May-2013 by Keseler I , SRI International

Enzymatic reaction of: peptidyl prolyl cis-trans isomerase

Synonyms: peptidylprolyl isomerase, PPIase, rotamase

EC Number:

a [protein]-L-proline (ω = 180) <=> a [protein]-L-proline (ω = 0)

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Reversibility of this reaction is unspecified.

The apparent Kcat/KM value in a protease-free assay is 2.8x106 M-1s-1 [Zoldak09]. The substrate specificity of the enzyme was measured using a library of fluorescent peptides, showing high activity with hydrophobic residues such as Leu, Tyr, and Phe [Zoldak09].

Kinetic Parameters:

Km (μM)
a [protein]-L-proline (ω = 180)

Sequence Features

Protein sequence of FKBP-type peptidyl prolyl cis-trans isomerase with features indicated

Feature Class Location Citations Comment
Protein-Segment 1 -> 69
UniProt: PPIase first part; Sequence Annotation Type: region of interest;
Conserved-Region 1 -> 95
UniProt: PPIase FKBP-type;
Mutagenesis-Variant 42
[Zhang07c, UniProt15]
UniProt: Decrease in PPIase activity, but has little impact on chaperone activity and interaction with HypB. Almost complete loss of PPIase activity; when associated with Y-132.
Protein-Segment 76 -> 120
UniProt: IF-chaperone; Sequence Annotation Type: region of interest;
Protein-Segment 129 -> 151
UniProt: PPIase second part; Sequence Annotation Type: region of interest;
Mutagenesis-Variant 132
[Zhang07c, UniProt15]
UniProt: Almost complete loss of PPIase activity, but has little impact on chaperone activity and interaction with HypB; when associated with S-42.
Protein-Segment 141 -> 146
UniProt: Glu-rich (acidic); Sequence Annotation Type: compositionally biased region;
Protein-Segment 148 -> 179
UniProt: His-rich (basic); Sequence Annotation Type: compositionally biased region;
Protein-Segment 152 -> 196
UniProt: Metal-binding; Sequence Annotation Type: region of interest;
Protein-Segment 166 -> 194
UniProt: Gly-rich; Sequence Annotation Type: compositionally biased region;
Mutagenesis-Variant 167 -> 168
[Kaluarachchi09, UniProt11]
UniProt: Reduces nickel-binding capacity.
Metal-Binding-Site 167
UniProt: Nickel; Non-Experimental Qualifier: potential;
Metal-Binding-Site 168
UniProt: Nickel; Non-Experimental Qualifier: potential;
Mutagenesis-Variant 184 -> 185
[Kaluarachchi09, UniProt11]
UniProt: Reduces nickel-binding capacity.
Metal-Binding-Site 184
UniProt: Nickel; Non-Experimental Qualifier: potential;
Metal-Binding-Site 185
UniProt: Nickel; Non-Experimental Qualifier: potential;
Metal-Binding-Site 193
UniProt: Nickel; Non-Experimental Qualifier: potential;
Metal-Binding-Site 195
UniProt: Nickel; Non-Experimental Qualifier: potential;

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram


10/20/97 Gene b3349 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11663; confirmed by SwissProt match.


Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Bernhardt02: Bernhardt TG, Roof WD, Young R (2002). "The Escherichia coli FKBP-type PPIase SlyD is required for the stabilization of the E lysis protein of bacteriophage phi X174." Mol Microbiol 45(1);99-108. PMID: 12100551

BolanosGarcia06: Bolanos-Garcia VM, Davies OR (2006). "Structural analysis and classification of native proteins from E. coli commonly co-purified by immobilised metal affinity chromatography." Biochim Biophys Acta 1760(9);1304-13. PMID: 16814929

Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043

Butland06: Butland G, Zhang JW, Yang W, Sheung A, Wong P, Greenblatt JF, Emili A, Zamble DB (2006). "Interactions of the Escherichia coli hydrogenase biosynthetic proteins: HybG complex formation." FEBS Lett 580(2);677-81. PMID: 16412426

Chan11: Chan Chung KC, Zamble DB (2011). "Protein interactions and localization of the Escherichia coli accessory protein HypA during nickel insertion to [NiFe] hydrogenase." J Biol Chem 286(50);43081-90. PMID: 22016389

Chung11: Chung KC, Zamble DB (2011). "The Escherichia coli metal-binding chaperone SlyD interacts with the large subunit of [NiFe]-hydrogenase 3." FEBS Lett 585(2);291-4. PMID: 21185288

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Gaudet10: Gaudet P, Livstone M, Thomas P (2010). "Annotation inferences using phylogenetic trees." PMID: 19578431

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

Graubner07: Graubner W, Schierhorn A, Bruser T (2007). "DnaK plays a pivotal role in Tat targeting of CueO and functions beside SlyD as a general Tat signal binding chaperone." J Biol Chem 282(10);7116-24. PMID: 17215254

Han07a: Han KY, Song JA, Ahn KY, Park JS, Seo HS, Lee J (2007). "Solubilization of aggregation-prone heterologous proteins by covalent fusion of stress-responsive Escherichia coli protein, SlyD." Protein Eng Des Sel 20(11);543-9. PMID: 17971396

Haupt11: Haupt C, Weininger U, Kovermann M, Balbach J (2011). "Local and coupled thermodynamic stability of the two-domain and bifunctional enzyme SlyD from Escherichia coli." Biochemistry 50(34);7321-9. PMID: 21770389

Haupt11a: Haupt C, Patzschke R, Weininger U, Groger S, Kovermann M, Balbach J (2011). "Transient enzyme-substrate recognition monitored by real-time NMR." J Am Chem Soc 133(29);11154-62. PMID: 21661729

Hottenrott97: Hottenrott S, Schumann T, Pluckthun A, Fischer G, Rahfeld JU (1997). "The Escherichia coli SlyD is a metal ion-regulated peptidyl-prolyl cis/trans-isomerase." J Biol Chem 272(25);15697-701. PMID: 9188461

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Jakob09: Jakob RP, Zoldak G, Aumuller T, Schmid FX (2009). "Chaperone domains convert prolyl isomerases into generic catalysts of protein folding." Proc Natl Acad Sci U S A 106(48);20282-7. PMID: 19920179

Janowski97: Janowski B, Wollner S, Schutkowski M, Fischer G (1997). "A protease-free assay for peptidyl prolyl cis/trans isomerases using standard peptide substrates." Anal Biochem 252(2);299-307. PMID: 9344417

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Kaluarachchi09: Kaluarachchi H, Sutherland DE, Young A, Pickering IJ, Stillman MJ, Zamble DB (2009). "The Ni(II)-Binding Properties of the Metallochaperone SlyD." J Am Chem Soc 131(51):18489-500. PMID: 19947632

Kaluarachchi11: Kaluarachchi H, Siebel JF, Kaluarachchi-Duffy S, Krecisz S, Sutherland DE, Stillman MJ, Zamble DB (2011). "Metal selectivity of the Escherichia coli nickel metallochaperone, SlyD." Biochemistry 50(49);10666-77. PMID: 22047179

Kaluarachchi11a: Kaluarachchi H, Zhang JW, Zamble DB (2011). "Escherichia coli SlyD, more than a Ni(II) reservoir." Biochemistry 50(50);10761-3. PMID: 22085337

Kaluarachchi12: Kaluarachchi H, Altenstein M, Sugumar SR, Balbach J, Zamble DB, Haupt C (2012). "Nickel Binding and [NiFe]-Hydrogenase Maturation by the Metallochaperone SlyD with a Single Metal-Binding Site in Escherichia coli." J Mol Biol 417(1-2);28-35. PMID: 22310044

Knappe07: Knappe TA, Eckert B, Schaarschmidt P, Scholz C, Schmid FX (2007). "Insertion of a chaperone domain converts FKBP12 into a powerful catalyst of protein folding." J Mol Biol 368(5);1458-68. PMID: 17397867

Kovermann11: Kovermann M, Zierold R, Haupt C, Low C, Balbach J (2011). "NMR relaxation unravels interdomain crosstalk of the two domain prolyl isomerase and chaperone SlyD." Biochim Biophys Acta 1814(7);873-81. PMID: 21466862

Kovermann13: Kovermann M, Schmid FX, Balbach J (2013). "Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyD." Biol Chem 394(8);965-75. PMID: 23585180

Kovermann13a: Kovermann M, Balbach J (2013). "Dynamic control of the prolyl isomerase function of the dual-domain SlyD protein." Biophys Chem 171;16-23. PMID: 23268194

Leach07: Leach MR, Zhang JW, Zamble DB (2007). "The role of complex formation between the Escherichia coli hydrogenase accessory factors HypB and SlyD." J Biol Chem 282(22);16177-86. PMID: 17426034

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

Maratea85: Maratea D, Young K, Young R (1985). "Deletion and fusion analysis of the phage phi X174 lysis gene E." Gene 40(1);39-46. PMID: 2936651

Martino09: Martino L, He Y, Hands-Taylor KL, Valentine ER, Kelly G, Giancola C, Conte MR (2009). "The interaction of the Escherichia coli protein SlyD with nickel ions illuminates the mechanism of regulation of its peptidyl-prolyl isomerase activity." FEBS J 276(16);4529-44. PMID: 19645725

Martino09a: Martino L, Kelly G, Conte MR (2009). "Letter to the Editor: resonance assignment of SlyD from E. coli." Biomol NMR Assign 3(2);235-7. PMID: 19760519

Mendel06: Mendel S, Holbourn JM, Schouten JA, Bugg TD (2006). "Interaction of the transmembrane domain of lysis protein E from bacteriophage phiX174 with bacterial translocase MraY and peptidyl-prolyl isomerase SlyD." Microbiology 152(Pt 10);2959-67. PMID: 17005977

Mitterauer99: Mitterauer T, Nanoff C, Ahorn H, Freissmuth M, Hohenegger M (1999). "Metal-dependent nucleotide binding to the Escherichia coli rotamase SlyD." Biochem J 342 ( Pt 1);33-9. PMID: 10432297

Mukherjee03: Mukherjee S, Shukla A, Guptasarma P (2003). "Single-step purification of a protein-folding catalyst, the SlyD peptidyl prolyl isomerase (PPI), from cytoplasmic extracts of Escherichia coli." Biotechnol Appl Biochem 37(Pt 2);183-6. PMID: 12630907

Roof94: Roof WD, Horne SM, Young KD, Young R (1994). "slyD, a host gene required for phi X174 lysis, is related to the FK506-binding protein family of peptidyl-prolyl cis-trans-isomerases." J Biol Chem 269(4);2902-10. PMID: 8300625

Roof97: Roof WD, Fang HQ, Young KD, Sun J, Young R (1997). "Mutational analysis of slyD, an Escherichia coli gene encoding a protein of the FKBP immunophilin family." Mol Microbiol 25(6);1031-46. PMID: 9350861

Scholz06: Scholz C, Eckert B, Hagn F, Schaarschmidt P, Balbach J, Schmid FX (2006). "SlyD proteins from different species exhibit high prolyl isomerase and chaperone activities." Biochemistry 45(1);20-33. PMID: 16388577

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProt15: UniProt Consortium (2015). "UniProt version 2015-01 released on 2015-01-16 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

Weininger09: Weininger U, Haupt C, Schweimer K, Graubner W, Kovermann M, Bruser T, Scholz C, Schaarschmidt P, Zoldak G, Schmid FX, Balbach J (2009). "NMR solution structure of SlyD from Escherichia coli: spatial separation of prolyl isomerase and chaperone function." J Mol Biol 387(2);295-305. PMID: 19356587

Witkowska12: Witkowska D, Valensin D, Rowinska-Zyrek M, Karafova A, Kamysz W, Kozlowski H (2012). "Coordination of Ni(2+) and Cu(2+) to metal ion binding domains of E. coli SlyD protein." J Inorg Biochem 107(1);73-81. PMID: 22178668

Wulfing94: Wulfing C, Lombardero J, Pluckthun A (1994). "An Escherichia coli protein consisting of a domain homologous to FK506-binding proteins (FKBP) and a new metal binding motif." J Biol Chem 269(4);2895-901. PMID: 8300624

Zhang05c: Zhang JW, Butland G, Greenblatt JF, Emili A, Zamble DB (2005). "A role for SlyD in the Escherichia coli hydrogenase biosynthetic pathway." J Biol Chem 280(6);4360-6. PMID: 15569666

Zhang07c: Zhang JW, Leach MR, Zamble DB (2007). "The peptidyl-prolyl isomerase activity of SlyD is not required for maturation of Escherichia coli hydrogenase." J Bacteriol 189(21);7942-4. PMID: 17720786

Zoldak09: Zoldak G, Aumuller T, Lucke C, Hritz J, Oostenbrink C, Fischer G, Schmid FX (2009). "A library of fluorescent peptides for exploring the substrate specificities of prolyl isomerases." Biochemistry 48(43);10423-36. PMID: 19785464

Zoldak09a: Zoldak G, Carstensen L, Scholz C, Schmid FX (2009). "Consequences of domain insertion on the stability and folding mechanism of a protein." J Mol Biol 386(4);1138-52. PMID: 19136015

Zoldak11: Zoldak G, Schmid FX (2011). "Cooperation of the prolyl isomerase and chaperone activities of the protein folding catalyst SlyD." J Mol Biol 406(1);176-94. PMID: 21147124

Zoldak13: Zoldak G, Geitner AJ, Schmid FX (2013). "The prolyl isomerase SlyD is a highly efficient enzyme but decelerates the conformational folding of a client protein." J Am Chem Soc 135(11);4372-9. PMID: 23445547

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.0 on Fri Sep 4, 2015, biocyc14.