The IsdG-family of haem oxygenases degrades haem to a novel chromophore - Wikidata - awgldk - TriplyDB

The IsdG-family of haem oxygenases degrades haem to a novel chromophore

The IsdG-family of haem oxygenases degrades haem to a novel chromophore

http://www.wikidata.org/entity/Q27660036

about

Formaldehyde Stress Responses in Bacterial Pathogens Crystallographic and Spectroscopic Insights into Heme Degradation by Mycobacterium tuberculosis MhuD Inactivation of the Heme Degrading Enzyme IsdI by an Active Site Substitution That Diminishes Heme Ruffling In vitro heme biotransformation by the HupZ enzyme from Group A streptococcus Bacillus subtilis Fur represses one of two paralogous haem-degrading monooxygenases.Substrate, product, and cofactor: The extraordinarily flexible relationship between the CDE superfamily and heme Heme uptake in bacterial pathogens IsdB-dependent hemoglobin binding is required for acquisition of heme by Staphylococcus aureus.Electronic properties of the highly ruffled heme bound to the heme degrading enzyme IsdI.Nutritional immunity: transition metals at the pathogen-host interface.Metal limitation and toxicity at the interface between host and pathogen Specificity for human hemoglobin enhances Staphylococcus aureus infection.The flexible loop of Staphylococcus aureus IsdG is required for its degradation in the absence of heme Staphylococcus lugdunensis IsdG liberates iron from host heme.The Escherichia coli protein YfeX functions as a porphyrinogen oxidase, not a heme dechelatase Nfu facilitates the maturation of iron-sulfur proteins and participates in virulence in Staphylococcus aureus.Protein secretion and surface display in Gram-positive bacteria.The TB Structural Genomics Consortium: a decade of progress.Structure-based Mechanistic Insights into Terminal Amide Synthase in Nosiheptide-Represented Thiopeptides Biosynthesis The PRE-Derived NMR Model of the 38.8-kDa Tri-Domain IsdH Protein from Staphylococcus aureus Suggests That It Adaptively Recognizes Human Hemoglobin.Evolutionary relationships between heme-binding ferredoxin α + β barrels.Dynamic ruffling distortion of the heme substrate in non-canonical heme oxygenase enzymes.Time-resolved Studies of IsdG Protein Identify Molecular Signposts along the Non-canonical Heme Oxygenase Pathway A new way to degrade heme: the Mycobacterium tuberculosis enzyme MhuD catalyzes heme degradation without generating CO.Unique coupling of mono- and dioxygenase chemistries in a single active site promotes heme degradation.Heme degradation by Staphylococcus aureus IsdG and IsdI liberates formaldehyde rather than carbon monoxide.Iron in infection and immunity.A battle for iron: host sequestration and Staphylococcus aureus acquisition Metal ion acquisition in Staphylococcus aureus: overcoming nutritional immunity.Molecular mechanisms of Staphylococcus aureus iron acquisition.Sequestration and scavenging of iron in infection.Structures of the substrate-free and product-bound forms of HmuO, a heme oxygenase from corynebacterium diphtheriae: x-ray crystallography and molecular dynamics investigation.Radical new paradigm for heme degradation in Escherichia coli O157:H7.Recent advances in bacterial heme protein biochemistry.The theft of host heme by Gram-positive pathogenic bacteria.Recent developments in understanding the iron acquisition strategies of gram positive pathogens.Chlamydomonas reinhardtii LFO1 Is an IsdG Family Heme Oxygenase.Reaction intermediates in the heme degradation reaction by HutZ from Vibrio cholerae.Heme Synthesis and Acquisition in Bacterial Pathogens.Tight binding of heme to Staphylococcus aureus IsdG and IsdI precludes design of a competitive inhibitor.

P2860

Q26765935-3123BE55-0BF1-41DB-A8C0-3F14767CD16F Q27644563-92DD5C30-D2EA-4C26-A825-A7207D06CCC3 Q27671517-847EAC30-E88D-4B37-B69C-91DB1B05AD83 Q27704826-E2576C6F-1E27-49B8-9311-E40F85F62EB8 Q29346701-81EFB354-2BA0-4FAD-994C-94B6EA3F5F5B Q30152968-C1510D23-6C04-4B4F-BC73-08851CA39302 Q33555758-3311A5DE-D812-444F-AEF3-CBD2DB5F4924 Q33687709-D2C58D4C-1D8D-46A3-97B6-5EE8CDE19D89 Q33970868-0AF16102-9282-4E30-AF99-A2625252947F Q34288184-2657580E-40D5-43C6-AE1E-BFEC0AAFDCC3 Q34490463-A69F9791-001E-4068-8CD4-B02620B65235 Q34545943-1F99D148-3500-487F-9F37-328CCF6C85DF Q35146302-45D03369-7873-465E-9D87-DE2579272B34 Q35192451-ACA133B1-1356-42D0-AF15-02932D9D882C Q35547977-40F09F68-BBA3-457D-B557-1D00A9C4B4F7 Q35596266-D8ED728E-0EF0-4777-BBF1-8C8CB77A76C6 Q35814726-6F991ECB-EBA2-4E82-A5E9-64B9BEAB5336 Q35846941-528B12B7-0476-46D2-A7D8-F3472D7551E1 Q35918017-08196FAB-B526-4DE4-8CFC-3BEDAC1CAA61 Q35956497-F238441A-9A97-40E5-B297-E6CAB0DD8B80 Q35992728-7B1DE6DC-7352-41E9-926B-745EA7F52C8F Q36044299-FBAD901B-4DD3-48AF-8863-05AE81AE5CDA Q36442427-910BC55F-9340-4072-9DD0-18C78C6FEBA1 Q36742120-33D38094-BF8E-44E6-B6AA-AC37A597EC45 Q36802518-91099D0B-875A-4EEF-9B94-2625B52DCDA3 Q36901582-96E8D0FA-8C24-4F26-9C80-03D642E780F5 Q36913895-741A3670-4CA5-408F-81EB-76F74D24A4CA Q37203020-1E5C46CB-88E1-4D08-A35D-2742FD09D237 Q37229481-6CC776D5-F51A-45B2-93EF-B6D41C035524 Q37254091-AA9F734F-0D07-49FB-A210-855B374280E2 Q37264669-30DA0488-F2C6-449F-A412-3909FB0946B5 Q37348889-01602873-ED91-4045-8548-A7B3AACA23CD Q37379819-ADAFCF4F-6AC3-482E-9E9B-3483D9A392D7 Q37845543-102AC202-A137-4C61-B1D1-7C19202B152B Q37897143-E008E1A8-20FD-4B0E-A9F6-94B9F789659D Q38415707-D43C9D6C-2562-4F68-B5C9-281515486DFB Q38621091-7A5565D2-6B01-440C-AD27-A32E9A6ED563 Q38728507-0246AE77-2D32-4BD3-8D0D-5C8E5706B160 Q38791019-5BCB69EB-CDB0-478B-9644-88739DE90C24 Q38840919-B377D6C4-57AE-459B-B4A1-C13876336917

P2860

The IsdG-family of haem oxygenases degrades haem to a novel chromophore

http://www.wikidata.org/entity/Q27660036

description

2010 nî lūn-bûn

@nan

2010 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի մարտին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

The IsdG-family of haem oxygenases degrades haem to a novel chromophore

@ast

The IsdG-family of haem oxygenases degrades haem to a novel chromophore

@en

The IsdG-family of haem oxygenases degrades haem to a novel chromophore

@nl

type

label

The IsdG-family of haem oxygenases degrades haem to a novel chromophore

@ast

The IsdG-family of haem oxygenases degrades haem to a novel chromophore

@en

The IsdG-family of haem oxygenases degrades haem to a novel chromophore

@nl

prefLabel

The IsdG-family of haem oxygenases degrades haem to a novel chromophore

@ast

The IsdG-family of haem oxygenases degrades haem to a novel chromophore

@en

The IsdG-family of haem oxygenases degrades haem to a novel chromophore

@nl

P1433

Q27660036-2581707B-9B4A-4757-8D54-6BC2B225388D

P1476

Q27660036-83B9EDF4-28BA-4A19-896D-32860AB83A4A

P2093

Q27660036-098E2881-7BC5-4D3B-8A10-478AA3736464

Q27660036-64257ECA-6D71-46BF-B2F8-DB132BC3D72F

Q27660036-778325A9-F2C6-4EB7-8DC0-759941855B1A

Q27660036-A6ED3EDA-0D6F-493D-9A76-54B192427604

Q27660036-DCE632F4-8E5D-4F63-9440-16032CAB5B35

Q27660036-DDEBE739-4481-4C43-9C70-ED7315F25D4D

P2860

Q27660036-00ABDBE0-682E-4037-BD28-240FE903C705

Q27660036-05331BC5-5C72-48F1-9EEE-ED22E12B7479

Q27660036-05960E63-9D82-4E10-8FC8-2679F7B4C0F5

Q27660036-0C9761AD-4A1E-4530-8E64-13BD4C7B715A

Q27660036-27E913BB-6656-4891-8401-F8897E5B0595

Q27660036-2884D19F-88AE-4A2B-B25B-ACB1349D778F

Q27660036-2EC0297C-CF40-4004-832F-732828E001F2

Q27660036-33AEFAB0-978C-4676-8845-F33CDF7C5BD2

Q27660036-33EDF20E-DCF2-4B76-AFFF-BCEEA8C73668

Q27660036-39722CA1-33B7-4300-A104-477B5FCD5950

P304

Q27660036-43ED2A7C-58D6-454B-AE76-9F2151114A57

P31

Q27660036-8E34D5EB-AA3E-4F6E-8883-A18E19F66A97

P3181

Q27660036-5B407100-E410-4C2E-A132-21C2BC851E33

P356

Q27660036-CF511F36-B984-4EC0-BBE7-FFCA4FDA21DF

P407

Q27660036-D86BD76A-4929-47D3-83D2-B7B2A0F1EE0E

P433

Q27660036-44919A71-DD9A-48B9-A1FF-7BF3047C0300

P478

Q27660036-66375320-1445-481A-9CB0-A4C3751CAD4F

P50

Q27660036-10A86D4D-7942-49E6-8672-556C8B6B9112

Q27660036-CDF24340-2A9F-438C-A63D-DD6FB54C6F70

Q27660036-E414999F-1BEF-4ADE-92D0-496FD383453F

P577

Q27660036-E75E26BC-B87F-428B-9C2C-9CC43F39B1D8

P5875

Q27660036-63730DC8-2C63-414F-988B-50BCB8B20C9B

P698

Q27660036-39ED03F2-CD45-41B5-98ED-CB7FA3CB9A49

P921

Q27660036-610DEA7B-C4C5-49A7-B3BA-9AE73277BFE3

Q27660036-783ECFE9-2528-48B0-9AC9-5FE6AA97BAF7

Q27660036-78BC137C-D77C-4AD5-867A-BDCF938734A6

Q27660036-C0595723-24EF-4A65-A3B6-82ACCCC0CAA1

P932

Q27660036-8AF8530A-D1C0-4BFA-8836-4D5DA4BF7728

P3181

P356

J.1365-2958.2010.07076.X

P1433

Molecular Microbiology

P1476

The IsdG-family of haem oxygenases degrades haem to a novel chromophore

@en

P2093

Brian O Bachmann

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

David W Wright

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

Donald F Stec

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

Georgia N Ukpabi

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

Robert Krull

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

S Reese Harry

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

P2860

Crystal structure of rat heme oxygenase-1 in complex with heme

Crystal structure of heme oxygenase from the gram-negative pathogen Neisseria meningitidis and a comparison with mammalian heme oxygenase-1

Crystal structures of the NO- and CO-bound heme oxygenase from Neisseriae meningitidis. Implications for O2 activation

Crystal structures of the ferric, ferrous, and ferrous-NO forms of the Asp140Ala mutant of human heme oxygenase-1: catalytic implications

Crystal structure of the dioxygen-bound heme oxygenase from Corynebacterium diphtheriae: implications for heme oxygenase function

Ruffling of Metalloporphyrins Bound to IsdG and IsdI, Two Heme-degrading Enzymes in Staphylococcus aureus

Unusual Diheme Conformation of the Heme-Degrading Protein from Mycobacterium tuberculosis

A graphical user interface to the CCP4 program suite

Refinement of macromolecular structures by the maximum-likelihood method

Scaling and assessment of data quality

P304

1529-1538

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

P31

scholarly article

P3181

2257261

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

P356

10.1111/J.1365-2958.2010.07076.X

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

P407

P433

6

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

P478

75

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

P50

Michelle L Reniere

P577

2010-02-17T00:00:00Z

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

P5875

41561207

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

P698

20180905

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

P921

5-oxo-delta-bilirubin(2-)

15-oxo-beta-bilirubin(2-)

5-oxo-delta-bilirubin

15-oxo-beta-bilirubin

P932

3800195

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