Seems that the answer is no.
"Although 4-hydroxyproline, the proline
congener abundant in mammalian species, is
structurally similar to proline, its metabolism
is distinctly different (2). A critical contributor
to the physical structure of organisms, hydrox-yproline is not found in species before the evo-lution of metazoans. Preformed hydroxypro-line is not incorporated into protein presumably
because all the triplet codons were occupied
(2, 52). Instead, it is formed by the posttransla-tional hydroxylation of proline in proteins (2).
Since hydroxyproline is not recycled for pro-tein synthesis, its degradation continues down
to 2- and 3-carbon compounds. The degrada-tive pathway, however, shares some of the en-zymes metabolizing proline (103). The ini-tial step is catalyzed by hydroxyproline oxidase
(PRODH2), an enzyme encoded by a gene dis-tinct from that for proline oxidase ( PRODH)
and with little overlap in substrate utilization
(91). In contrast, in the second step of their
degradation, hydroxyproline and proline share
the same enzyme, i.e., P5C dehydrogenase
(103). It is interesting that P5C reductase from
animals not only converts P5C back to proline
for protein synthesis, but also can reduce OH-P5C to hydroxyproline even though product
hydroxyproline is not reused for protein synthe-sis (3). P5C reductase in prokaryotes, however,
does not have this activity for OH-P5C (3)."