Enone-promoted decarboxylation of trans-4-hydroxy-l-proline in flow: a side-by-side comparison to batch

2021 ◽  
Author(s):  
Rowan L. Pilkington ◽  
Madeleine A. Dallaston ◽  
G. Paul Savage ◽  
Craig M. Williams ◽  
Anastasios Polyzos
Keyword(s):  
Hydroxy Proline

An efficient and scalable enone-promoted method for the decarboxylation of trans-4-hydroxy-proline has been developed in flow to provide access to (R)-pyrrolidin-3-ol hydrochloride using biomass-derived isophorone.

Oxydoréduction photochimique et thermique entre le chrome(VI) et un acide α aminé (glycine, alanine, hydroxy proline et méthionine)

1986 ◽  
Vol 64 (9) ◽  
pp. 1864-1869 ◽  
Author(s):  
M. Bolte ◽  
B. Robert ◽  
J. Lemaire
Keyword(s):  
Amino Acid ◽  
Spectroscopic Studies ◽  
Quantum Yields ◽  
Charge Transfer Reaction ◽  
Acid Complex ◽  
Protonated Amino Acid ◽  
Chromium Vi ◽  
Hydroxy Proline ◽  
Amino Acid Formula ◽  
Rule Out

Photochemical and thermal oxidation that occurs between chromium(VI) and various amino acids leads quantitatively to chromium(III). Spectroscopic studies rule out the formation of a chromium(VI) – amino acid complex in the ground state. Thermal oxidoreduction involves HCrO4−, the protonated amino acid [Formula: see text] and H+ ions. Chromium(V) appears to be an intermediate species in the reaction. HCrO4− is the only absorbing compound and the photochemical chromium(VI) reduction proceeds through a reaction between [HCrO4−]* and the amino acid. Chromium(V) is the primary product of the charge transfer reaction. Reduction quantum yields are proportional to the amino acid concentration and pH independent in the HCrO4− existence range.

Saccharopolytide A, a new cyclic tetrapeptide with rare 4-hydroxy-proline moieties from the deep-sea derived actinomycete Saccharopolyspora cebuensis MCCC 1A09850

2017 ◽  
Vol 32 (14) ◽  
pp. 1627-1631 ◽  
Author(s):  
Chun-Lan Xie ◽  
Siwen Niu ◽  
Jin-Mei Xia ◽  
Kun Peng ◽  
Gai-Yun Zhang ◽  
...  
Keyword(s):  
Deep Sea ◽  
Hydroxy Proline ◽  
Cyclic Tetrapeptide

Cyclic hydroxycarboxylic acids. III. Tosylation studies on Mono- and Di-hydroxycyclopentanecarboxylates and Mono- and Di-hydroxyprolines

1977 ◽  
Vol 30 (1) ◽  
pp. 131 ◽  
Author(s):  
RP Philp ◽  
AV Robertson
Keyword(s):  
Free Amino ◽  
Heterogeneous System ◽  
Methyl Esters ◽  
Hydroxyl Groups ◽  
Large Excess ◽  
Molar Ratios ◽  
Tosyl Chloride ◽  
Hydroxycarboxylic Acids ◽  
Hydroxy Proline ◽  
Cis And Trans

A large excess of reagent is needed for satisfactory ditosylation of methyl c-2,t-3- and t-2,c-3-di-hydroxycyclopentane-r-1-carboxylates using tosyl chloride-pyridine at 5° overnight. With less reagent, mixtures are produced from which one monotosyl derivative of the t-2,c- 3-series was isolated and its structure proved. By contrast, the methyl cis- and trans-2-hydroxycyclopentanecarboxylates readily tosylate with normal molar ratios of reagent. In the proline series ditosylation of 2,3-trans- 3,4-cis-3,4-dihydroxy-N-tosylproline methyl ester occurs normally in tosyl chloride-pyridine, and so does tosylation of both cis- and trans-4-hydroxy-N-tosylproline methyl esters. On the other hand tosylation of the 3-hydroxy counterparts is very slow, although acetylation of these 3-hydroxyl groups proceeds normally. The O-tosylation results are striking for the lack of pattern. A comparison is also made of O-tosylation accompanying N-tosylation of the free amino acids cis- and trans-3-hydroxy-proline, cis- and trans- 4- hydroxyproline, and the two cis-glycols of 3,4-dihydroxyproline in the heterogeneous system tosyl chloride-ether-aqueous NaOH. Significant O- tosylation occurs in some cases but not in others. This correlation permits assignment of structure to a mono-O-tosyl derivative of a 3,4- dihydroxy-N-tosylproline obtained previously by us.

Unexpected racemization of proline or hydroxy-proline phenacyl ester during coupling reactions with Boc-amino acids

2009 ◽  
Vol 40 (2) ◽  
pp. 114-118 ◽  
Author(s):  
HISAYA KURODA ◽  
SHIGERU KUBO ◽  
NAOYOSHI CHINO ◽  
TERUTOSHI KIMURA ◽  
SHUMPEI SAKAKIBARA
Keyword(s):  
Amino Acids ◽  
Coupling Reactions ◽  
Hydroxy Proline ◽  
Phenacyl Ester

scholarly journals Core Glycosylation of Collagen Is Initiated by Two β(1-O)Galactosyltransferases

2008 ◽  
Vol 29 (4) ◽  
pp. 943-952 ◽  
Author(s):  
Belinda Schegg ◽  
Andreas J. Hülsmeier ◽  
Christoph Rutschmann ◽  
Charlotte Maag ◽  
Thierry Hennet
Keyword(s):  
Biological Significance ◽  
Protein Sequencing ◽  
Helix Formation ◽  
Left Handed ◽  
Hydroxy Proline ◽  
Mannose Binding ◽  
Triple Helix Formation ◽  
Lysine Residues ◽  
Low Levels ◽  
Binding Lectin

ABSTRACT Collagen is a trimer of three left-handed alpha chains representing repeats of the motif Gly-X-Y, where (hydroxy)proline and (hydroxy)lysine residues are often found at positions X and Y. Selected hydroxylysines are further modified by the addition of galactose and glucose-galactose units. Collagen glycosylation takes place in the endoplasmic reticulum before triple-helix formation and is mediated by β(1-O)galactosyl- and α(1-2)glucosyltransferase enzymes. We have identified two collagen galactosyltransferases using affinity chromatography and tandem mass spectrometry protein sequencing. The two collagen β(1-O)galactosyltransferases corresponded to the GLT25D1 and GLT25D2 proteins. Recombinant GLT25D1 and GLT25D2 enzymes showed a strong galactosyltransferase activity toward various types of collagen and toward the serum mannose-binding lectin MBL, which contains a collagen domain. Amino acid analysis of the products of GLT25D1 and GLT25D2 reactions confirmed the transfer of galactose to hydroxylysine residues. The GLT25D1 gene is constitutively expressed in human tissues, whereas the GLT25D2 gene is expressed only at low levels in the nervous system. The GLT25D1 and GLT25D2 enzymes are similar to CEECAM1, to which we could not attribute any collagen galactosyltransferase activity. The GLT25D1 and GLT25D2 genes now allow addressing of the biological significance of collagen glycosylation and the importance of this posttranslational modification in the etiology of connective tissue disorders.

scholarly journals Cell-wall lytic enzymes (autolysins) of Chlamydomonas reinhardtii are (hydroxy)proline-specific proteases

1987 ◽  
Vol 170 (1-2) ◽  
pp. 485-491 ◽  
Author(s):  
Lothar JAENICKE ◽  
Wolfgang KUHNE ◽  
Rainer SPESSERT ◽  
Ursula WAHLE ◽  
Sabine WAFFENSCHMIDT
Keyword(s):  
Cell Wall ◽  
Chlamydomonas Reinhardtii ◽  
Lytic Enzymes ◽  
Hydroxy Proline ◽  
Cell Wall Lytic Enzymes

scholarly journals Enrichment of Larval Fish Feed with Free Amino Acids and Proteins by Coating with Lactobacillus paracasei subsp. paracasei BGHN14 Homogenate

2021 ◽  
Vol 21 (11) ◽  
pp. 569-573
Author(s):  
Jovanka Lukić ◽  
Nemanja Stanisavljević ◽  
Goran Vukotić ◽  
Amarela Terzić-Vidojević ◽  
Jelena Begović ◽  
...  
Keyword(s):  
Amino Acid ◽  
Free Amino ◽  
Larval Fish ◽  
Lactobacillus Paracasei ◽  
Total Amino Acid ◽  
Fish Feed ◽  
Hydroxy Proline ◽  
Growth Promoting ◽  
Animal Feedstuffs ◽  
Feed Samples

This research aimed to test whether coating with Lactobacillus paracasei subsp. paracasei BGHN14 homogenate may increase soluble protein and amino acid amount on larval fish feed surface. Total amino acid and protein, as well as taste stimulating and growth promoting amino acid amounts were analyzed in coated feed samples. Results indicated that coating with BGHN14 homogenate increased the amount of soluble proteins and free Glycine on feed surface, as well as the availability of protein-bound (hydroxy-)Proline. This lab-scale research provides the basis for use of lactobacilli as resource efficient source of soluble nutrients for animal feedstuffs.

Sign in / Sign up

Export Citation Format

Share Document