R C Holz
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Explore the profile of R C Holz including associated specialties, affiliations and a list of published articles.
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Articles
17
Citations
213
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Recent Articles
1.
Vanek V, Picha J, Budesinsky M, Sanda M, Jiracek J, Holz R, et al.
Protein Pept Lett
. 2009 Dec;
17(3):405-9.
PMID: 19958280
The search for potential inhibitors that target so far unexplored bacterial enzyme mono-N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE) has stimulated a development of methodology for quick and efficient preparation of mono-N-acylated 2,6-diaminopimelic...
2.
Hlavacek J, Picha J, Vanek V, Jiracek J, Slaninova J, Fucik V, et al.
Amino Acids
. 2009 Aug;
38(4):1155-64.
PMID: 19649769
A series of N (alpha)-acyl (alkyl)- and N (alpha)-alkoxycarbonyl-derivatives of L- and D-ornithine were prepared, characterized, and analyzed for their potency toward the bacterial enzyme N (alpha)-acetyl-L-ornithine deacetylase (ArgE). ArgE...
3.
Cosper N, Dsouza V, Scott R, Holz R
Biochemistry
. 2001 Oct;
40(44):13302-9.
PMID: 11683640
The Co and Fe K-edge extended X-ray absorption fine structure (EXAFS) spectra of the methionyl aminopeptidase from Escherichia coli (EcMetAP) have been recorded in the presence of 1 and 2...
4.
Stamper C, Bennett B, Edwards T, Holz R, Ringe D, Petsko G
Biochemistry
. 2001 Jun;
40(24):7035-46.
PMID: 11401547
The nature of the interaction of the transition-state analogue inhibitor L-leucinephosphonic acid (LPA) with the leucine aminopeptidase from Aeromonas proteolytica (AAP) was investigated. LPA was shown to be a competitive...
5.
Dsouza V, Bennett B, Copik A, Holz R
Biochemistry
. 2000 Mar;
39(13):3817-26.
PMID: 10736182
The metal-binding properties of the methionyl aminopeptidase from Escherichia coli (MetAP) were investigated. Measurements of catalytic activity as a function of added Co(II) and Fe(II) revealed that maximal enzymatic activity...
6.
Bienvenue D, Bennett B, Holz R
J Inorg Biochem
. 2000 Mar;
78(1):43-54.
PMID: 10714704
The peptide inhibitor L-leucinethiol (LeuSH) was found to be a potent, slow-binding inhibitor of the aminopeptidase from Aeromonas proteolytica (AAP). The overall potency (K(I)*) of LeuSH was 7 nM while...
7.
Huntington K, Bienvenue D, Wei Y, Bennett B, Holz R, Pei D
Biochemistry
. 1999 Nov;
38(47):15587-96.
PMID: 10569943
Peptide-derived thiols of the general structure N-mercaptoacyl-leucyl-p-nitroanilide (1a-c) were synthesized and found to be potent, slow-binding inhibitors of the aminopeptidase from Aeromonas proteolytica (AAP). The overall potencies (K(I)) of these...
8.
Ustynyuk L, Bennett B, Edwards T, Holz R
Biochemistry
. 1999 Sep;
38(35):11433-9.
PMID: 10471294
Seven aliphatic and two aromatic alcohols were tested as reporters of the substrate selectivity of the aminopeptidase from Aeromonas proteolytica (AAP). This series of alcohols was chosen to systematically probe...
9.
Holz R, Alvarez M, Zumft W, Dooley D
Biochemistry
. 1999 Aug;
38(34):11164-71.
PMID: 10460173
1H NMR spectra of the CuA center of N2OR from Pseudomonas stutzeri, and a mutant enzyme that contains only CuA, were recorded in both H2O- and D2O-buffered solution at pH...
10.
Dsouza V, Holz R
Biochemistry
. 1999 Aug;
38(34):11079-85.
PMID: 10460163
The identity of the physiologically relevant metal ions for the methionyl aminopeptidase (MetAP) from Escherichia coli was investigated and is suggested to be Fe(II). The metal content of whole cells...