Crystal Structures and Kinetics of Monofunctional Proline Dehydrogenase Provide Insight into Substrate Recognition and Conformational Changes Associated with Flavin Reduction and Product Release - Wikidata - awgldk - TriplyDB

Crystal Structures and Kinetics of Monofunctional Proline Dehydrogenase Provide Insight into Substrate Recognition and Conformational Changes Associated with Flavin Reduction and Product Release

Crystal Structures and Kinetics of Monofunctional Proline Dehydrogenase Provide Insight into Substrate Recognition and Conformational Changes Associated with Flavin Reduction and Product Release

http://www.wikidata.org/entity/Q27675129

about

Structures of the PutA peripheral membrane flavoenzyme reveal a dynamic substrate-channeling tunnel and the quinone-binding site Characterization of the proline-utilization pathway in Mycobacterium tuberculosis through structural and functional studies A covalent adduct of MbtN, an acyl-ACP dehydrogenase from Mycobacterium tuberculosis, reveals an unusual acyl-binding pocket Structures of Proline Utilization A Reveal the Fold and Functions of the Aldehyde Dehydrogenase Superfamily Domain of Unknown Function Involvement of proline oxidase (PutA) in programmed cell death of Xanthomonas.First evidence for substrate channeling between proline catabolic enzymes: a validation of domain fusion analysis for predicting protein-protein interactions.Kinetic and isotopic characterization of L-proline dehydrogenase from Mycobacterium tuberculosis.Evidence for hysteretic substrate channeling in the proline dehydrogenase and Δ1-pyrroline-5-carboxylate dehydrogenase coupled reaction of proline utilization A (PutA).Engineering a trifunctional proline utilization A chimaera by fusing a DNA-binding domain to a bifunctional PutA.Biophysical investigation of type A PutAs reveals a conserved core oligomeric structure.Structure, function, and mechanism of proline utilization A (PutA).Proline dehydrogenase from Thermus thermophilus does not discriminate between FAD and FMN as cofactor.Redox-dependent substrate-cofactor interactions in the Michaelis-complex of a flavin-dependent oxidoreductase.Structural Basis for the Substrate Inhibition of Proline Utilization A by Proline.Functional Impact of the N-terminal Arm of Proline Dehydrogenase from Thermus thermophilus.Structure and characterization of a class 3B proline utilization A: Ligand-induced dimerization and importance of the C-terminal domain for catalysis.The Proline Cycle As a Potential Cancer Therapy Target.Crystal structures of FMN-bound and FMN-free forms of dihydroorotate dehydrogenase from Trypanosoma brucei.High yields of active Thermus thermophilus proline dehydrogenase are obtained using maltose-binding protein as a solubility tag.

P2860

d03bad2b518217062910fd72214ee535e41a0237 e2fb8ad4417016603f67b0b60466f925355ea71b

P248

Q27681821-D78436E2-F419-426C-BEAB-05FDA2682453 Q27689784-AAC634C1-05BA-45DC-A135-9BAC0AE18E8A Q27700114-63E424E6-9D0F-4D0A-849B-974573A24577 Q27728132-EA26AF71-870A-45CF-9FA8-BBD50C6A4D66 Q33553420-9F57EEC2-9E55-4E73-BFFE-96926C065A90 Q35002908-0880F891-F26B-4CC0-9606-723007E60092 Q37339532-F39905F3-FCB6-4EB1-8834-E46C4C573C4A Q37563541-9A9A28CA-3236-492C-A47A-B6D9ACA43FB2 Q37626806-3433031F-8ED4-4C2D-9CD5-19FAC0202DB9 Q38677885-3700D0FA-C818-4583-B3AF-FA0094784EBD Q39437714-FCEEF60C-7C6C-4760-A920-4E0F32DFEB3F Q42318672-6FD45E13-9A2F-44F5-A68F-D45D4942798B Q47146237-809C25BF-7AD7-4420-A837-9E683013A624 Q47218650-5D6BAFCE-2916-459B-95F0-69A1F3E201F9 Q47654441-E4E446AC-3DE9-40B3-BD8E-F463A65702B1 Q51050542-C5A3827A-8B6A-4B23-858F-0389A48921BA Q52592104-A548A983-B1F9-430C-B4CC-C2153E7B19FD Q53831430-90D636A0-9E51-45DA-B491-ED6B8F3B92BA Q54276023-F776DC02-F1CB-4B3D-9C14-1183E2834BCC

P2860

Crystal Structures and Kinetics of Monofunctional Proline Dehydrogenase Provide Insight into Substrate Recognition and Conformational Changes Associated with Flavin Reduction and Product Release

http://www.wikidata.org/entity/Q27675129

description

2012 nî lūn-bûn

@nan

2012 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

name

Crystal Structures and Kinetic ...... Reduction and Product Release

@ast

Crystal Structures and Kinetic ...... Reduction and Product Release

@en

Crystal Structures and Kinetic ...... Reduction and Product Release

@nl

type

label

Crystal Structures and Kinetic ...... Reduction and Product Release

@ast

Crystal Structures and Kinetic ...... Reduction and Product Release

@en

Crystal Structures and Kinetic ...... Reduction and Product Release

@nl

prefLabel

Crystal Structures and Kinetic ...... Reduction and Product Release

@ast

Crystal Structures and Kinetic ...... Reduction and Product Release

@en

Crystal Structures and Kinetic ...... Reduction and Product Release

@nl

P1433

Q27675129-E59CCCFA-429F-4CFC-8A99-6343724A09E4

P1476

Q27675129-5E232866-2D6E-4791-B2E1-00606D08B535

P2093

Q27675129-1F399826-BDDF-4CEB-8B2D-B04508C541DD

Q27675129-363B831E-F5C1-40C8-A30C-1F4181BEFF81

Q27675129-5C60ED24-189E-4E3A-865E-71B3827A3CA0

Q27675129-AB6248E5-6A8E-4EB8-9F8D-00BE4ACAA56D

P2860

Q27675129-15EB2501-C97D-4329-BC15-DDE1A793DC18

Q27675129-249A7DE4-7969-4E10-BBC6-A618A1F3D637

Q27675129-25704D06-CE5E-4433-AC1F-23CCAE7A8D3D

Q27675129-26256EEE-8C7F-478B-9429-A4E710646308

Q27675129-2959FDE8-875F-451A-8282-EFBD1FB72F42

Q27675129-2977ECFF-C2E8-4B1D-AF08-C0808FFBBE6E

Q27675129-4BF0554C-5F17-4271-B0D5-7E24AAACAAB0

Q27675129-4C9E3AEE-0AA4-4AE6-BAD1-F2E8D6FCB772

Q27675129-53220BF2-7B05-4CEF-82FC-15E84881873C

Q27675129-578B1C3D-7C42-4DE7-B3C8-05FD3238C075

P304

Q27675129-119E5F12-06D2-444B-BEDD-73180642359E

P31

Q27675129-7D46BDC9-3947-46E0-9378-66796CD05783

P356

Q27675129-6640022A-D769-4934-AE02-1EBF7A3C418B

P407

Q27675129-E6E010CE-C157-49D3-9336-693EE1C78E04

P433

Q27675129-FE1D1CF5-44D3-4988-A43E-680029563EE9

P478

Q27675129-A105A1F6-20F0-40C1-8D69-596B5A7BEAA1

P50

Q27675129-C99AC60A-982E-40A8-A9E9-251246AEF91D

P577

Q27675129-9DF66CBA-0C1A-4852-9483-C2E3F0216BAF

P698

Q27675129-65907067-F5C3-4DBB-A2DC-3590685DC3C3

P921

Q27675129-20F64E7B-A5AF-4F18-B2B7-0838D26F4A9D

P932

Q27675129-B539AFB3-6194-4DAB-91E3-F827C04D50A6

P356

P1433

P1476

Crystal structures and kinetic ...... reduction and product release

@en

P2093

Benjamin W Arentson

http://www.w3.org/2001/XMLSchema#string

Dhiraj Srivastava

http://www.w3.org/2001/XMLSchema#string

Donald F Becker

http://www.w3.org/2001/XMLSchema#string

Min Luo

http://www.w3.org/2001/XMLSchema#string

P2860

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein

Redox-Induced Changes in Flavin Structure and Roles of Flavin N(5) and the Ribityl 2‘-OH Group in Regulating PutA−Membrane Binding † , ‡

Structure and Kinetics of Monofunctional Proline Dehydrogenase from Thermus thermophilus

Structural Basis for the Inactivation of Thermus thermophilus Proline Dehydrogenase by N- Propargylglycine † , ‡

A Conserved Active Site Tyrosine Residue of Proline Dehydrogenase Helps Enforce the Preference for Proline over Hydroxyproline as the Substrate † ‡

The Structure of the Proline Utilization A Proline Dehydrogenase Domain Inactivated by N -Propargylglycine Provides Insight into Conformational Changes Induced by Substrate Binding and Flavin Reduction ,

Crystal structure of the bifunctional proline utilization A flavoenzyme from Bradyrhizobium japonicum

Coot: model-building tools for molecular graphics

P304

10099-10108

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1021/BI301312F

http://www.w3.org/2001/XMLSchema#string

P407

P433

50

http://www.w3.org/2001/XMLSchema#string

P478

51

http://www.w3.org/2001/XMLSchema#string

P50

P577

2012-12-05T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

23151026

http://www.w3.org/2001/XMLSchema#string

P921

crystal structure

P932

3525754

http://www.w3.org/2001/XMLSchema#string