(Q37120622)

English

Dissecting the total transition state stabilization provided by amino acid side chains at orotidine 5'-monophosphate decarboxylase: a two-part substrate approach

scientific article published on 04 July 2008

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

Dissecting the total transition state stabilization provided by amino acid side chains at orotidine 5'-monophosphate decarboxylase: a two-part substrate approach (English)

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

John P. Richard

object named as

John P Richard

5

0 references

4

object named as

John A Gerlt

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

author name string

Shonoi A Barnett

1

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

Tina L Amyes

2

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

Bryant M Wood

3

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

language of work or name

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publication date

4 July 2008

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

47

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

30

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

7785-7787

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

A substrate in pieces: allosteric activation of glycerol 3-phosphate dehydrogenase (NAD+) by phosphite dianion

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2652672

14 September 2017

Formation and stability of a vinyl carbanion at the active site of orotidine 5'-monophosphate decarboxylase: pKa of the C-6 proton of enzyme-bound UMP

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2652672

14 September 2017

OMP decarboxylase--An enigma persists

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2652672

14 September 2017

Enzymatic catalysis of proton transfer at carbon: activation of triosephosphate isomerase by phosphite dianion

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2652672

14 September 2017

On the attribution and additivity of binding energies

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2652672

14 September 2017

Catalytic proficiency: the unusual case of OMP decarboxylase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2652672

14 September 2017

Structural basis for the catalytic mechanism of a proficient enzyme: orotidine 5'-monophosphate decarboxylase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2652672

14 September 2017

The crystal structure and mechanism of orotidine 5'-monophosphate decarboxylase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2652672

14 September 2017

Electrostatic stress in catalysis: Structure and mechanism of the enzyme orotidine monophosphate decarboxylase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2652672

14 September 2017

Anatomy of a proficient enzyme: The structure of orotidine 5'-monophosphate decarboxylase in the presence and absence of a potential transition state analog

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2652672

14 September 2017

Activation of orotidine 5'-monophosphate decarboxylase by phosphite dianion: the whole substrate is the sum of two parts

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2652672

3 September 2018

Dissecting a charged network at the active site of orotidine-5'-phosphate decarboxylase.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2652672

3 September 2018

Yeast orotidine-5'-phosphate decarboxylase: steady-state and pre-steady-state analysis of the kinetic mechanism of substrate decarboxylation.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2652672

3 September 2018

Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteins

1 reference

https://pubmed.ncbi.nlm.nih.gov/18598058

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Analysis of the role of the KMSKS loop in the catalytic mechanism of the tyrosyl-tRNA synthetase using multimutant cycles

1 reference

https://pubmed.ncbi.nlm.nih.gov/18598058

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1021/BI800939K

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

ResearchGate publication ID

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