The alpha-glucuronidase, GlcA67A, of Cellvibrio japonicus utilizes the carboxylate and methyl groups of aldobiouronic acid as important substrate recognition determinants (Q27640780)

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scientific article (publication date: 30 May 2003)

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English	The alpha-glucuronidase, GlcA67A, of Cellvibrio japonicus utilizes the carboxylate and methyl groups of aldobiouronic acid as important substrate recognition determinants	scientific article (publication date: 30 May 2003)

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1 November 2019

The alpha-glucuronidase, GlcA67A, of Cellvibrio japonicus utilizes the carboxylate and methyl groups of aldobiouronic acid as important substrate recognition determinants (English)

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12654910%20AND%20SRC:MED&resulttype=core&format=json

1 November 2019

Cellvibrio japonicus

object named as

Cellvibrio japonicus

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based on heuristic

inferred from title

3

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12654910%20AND%20SRC:MED&resulttype=core&format=json

1 November 2019

Jeremy H. Lakey

5

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1 November 2019

6

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1 November 2019

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Tibor Nagy

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1 November 2019

Didier Nurizzo

2

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1 November 2019

Peter Biely

4

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1 November 2019

Harry J Gilbert

7

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1 November 2019

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publication date

24 March 2003

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1 November 2019

Journal of Biological Chemistry

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1 November 2019

278

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1 November 2019

22

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1 November 2019

20286-20292

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1 November 2019

Updating the sequence-based classification of glycosyl hydrolases

1 reference

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21 January 2018

The membrane-bound alpha-glucuronidase from Pseudomonas cellulosa hydrolyzes 4-O-methyl-D-glucuronoxylooligosaccharides but not 4-O-methyl-D-glucuronoxylan.

1 reference

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21 January 2018

alpha-D-glucuronidases from the xylanolytic thermophiles Clostridium stercorarium and Thermoanaerobacterium saccharolyticum

1 reference

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21 January 2018

STEREOCHEMISTRY AND THE MECHANISM OF ENZYMATIC REACTIONS

1 reference

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21 January 2018

The structural basis for catalysis and specificity of the Pseudomonas cellulosa alpha-glucuronidase, GlcA67A

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M302205200

21 January 2018

A chromogenic substrate for a beta-xylosidase-coupled assay of alpha-glucuronidase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M302205200

21 January 2018

Key residues in subsite F play a critical role in the activity of Pseudomonas fluorescens subspecies cellulosa xylanase A against xylooligosaccharides but not against highly polymeric substrates such as xylan.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M302205200

21 January 2018

Processing of X-ray diffraction data collected in oscillation mode

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M302205200

21 January 2018

Refinement of macromolecular structures by the maximum-likelihood method

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M302205200

21 January 2018

Automated protein model building combined with iterative structure refinement

1 reference

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21 January 2018

Biochemical characterization and identification of catalytic residues in alpha-glucuronidase from Bacillus stearothermophilus T-6.

1 reference

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21 January 2018

The active site of cellobiohydrolase Cel6A from Trichoderma reesei: the roles of aspartic acids D221 and D175

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M302205200

21 January 2018

The cellobiohydrolases of Trichoderma reesei: a review of indirect and direct evidence that their function is not just glycosidic bond hydrolysis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M302205200

21 January 2018

Substrate specificity in glycoside hydrolase family 10. Tyrosine 87 and leucine 314 play a pivotal role in discriminating between glucose and xylose binding in the proximal active site of Pseudomonas cellulosa xylanase 10A.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M302205200

21 January 2018

Xylan binding subsite mapping in the xylanase from Penicillium simplicissimum using xylooligosaccharides as cryo-protectant

1 reference

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21 January 2018

Identifiers

10.1074/JBC.M302205200

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Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12654910%20AND%20SRC:MED&resulttype=core&format=json

1 November 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12654910%20AND%20SRC:MED&resulttype=core&format=json

1 November 2019

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