(Q27732175)

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Differentiation and identification of the two catalytic metal binding sites in bovine lens leucine aminopeptidase by x-ray crystallography

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title

Differentiation and identification of the two catalytic metal binding sites in bovine lens leucine aminopeptidase by x-ray crystallography (English)

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main subject

X-ray crystallography

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author name string

H Kim

series ordinal

1

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W N Lipscomb

series ordinal

2

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language of work or name

English

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publication date

1 June 1993

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published in

Proceedings of the National Academy of Sciences of the United States of America

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volume

90

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page(s)

5006-10

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issue

11

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cites work

Molecular structure of leucine aminopeptidase at 2.7-A resolution

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PubMed Central

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20 March 2017

Leucine aminopeptidase: bestatin inhibition and a model for enzyme-catalyzed peptide hydrolysis

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PubMed Central

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20 March 2017

Crystallographic R factor refinement by molecular dynamics

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PubMed Central

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20 March 2017

Diffraction methods for biological macromolecules. Interactive computer graphics: FRODO

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7 April 2017

xerB, an Escherichia coli gene required for plasmid ColE1 site-specific recombination, is identical to pepA, encoding aminopeptidase A, a protein with substantial similarity to bovine lens leucine aminopeptidase

1 reference

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PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=46642

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29 September 2017

Structure determination and refinement of bovine lens leucine aminopeptidase and its complex with bestatin.

1 reference

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PubMed Central

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=46642

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29 September 2017

Protein crystallography at sub-zero temperatures: Cryo-protective mother liquors for protein crystals

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PubMed Central

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29 September 2017

Leucine aminopeptidase (bovine lens). Effect of pH on the relative binding of Zn2+ and Mg2+ to and on activation of the enzyme

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PubMed Central

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29 September 2017

Leucine aminopeptidase (bovine lens). The relative binding of cobalt and zinc to leucine aminopeptidase and the effect of cobalt substitution on specific activity

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PubMed Central

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2 June 2018

Repeated seeding technique for growing large single crystals of proteins

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12 December 2020

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Leucine aminopeptidase. V. Activation, specificity, and mechanism of action

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https://pubmed.ncbi.nlm.nih.gov/8506345

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12 December 2020

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Steady-state kinetics of hydrolysis of dansyl-peptide substrates by leucine aminopeptidase

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/8506345

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Leucine aminopeptidase: a zinc metloenzyme

1 reference

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/8506345

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Kinetic parameters of metal-substituted leucine aminopeptidase from bovine lens

1 reference

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/8506345

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Metal binding stoichiometry and mechanism of metal ion modulation of the activity of porcine kidney leucine aminopeptidase

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/8506345

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Crystallization of pig mitochondrial aspartate aminotransferase by seeding with crystals of the chicken mitochondrial isoenzyme

1 reference

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/8506345

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Preliminary X-ray study of leucine aminopeptidase (bpvine lens), and oligomeric metalloenzyme

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/8506345

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

DOI

10.1073/PNAS.90.11.5006

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ResearchGate publication ID

14693664

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(Q27732175)

Differentiation and identification of the two catalytic metal binding sites in bovine lens leucine aminopeptidase by x-ray crystallography

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